This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
R. M. Nalbandyan, Denaturated agents influence on ceruloplazmin EPR spectra parameters, Biofizika. 18:821 (1973) (Russ.).
E. K. Ruuge, T. M. Kerimov and A. V. Panemanglor, Lyophilic effect on animal cell free radicals, Biofizika. 21:124 (1976) (Russ.).
M. V. Orlova, Kinetics of human blood ceruloplasmin properties under the effect of microcurrents at acupuncture points (letter), Biofizika. 36:732 (1991) (Russ.).
M. Iu. Tarasev, E. P. Saburenkova, I. I. Dantsig, K. A. Moshkov and V. V. Ryl’kov, Effect of ceruloplasmin conformation on its activity: significance for clinical analysis, Vopr. Med. Khim. 37:43 (1991) (Russ.).
R. G. Saifutdinov, Blood plasma PMC in donors and patients, Magnitnyi Rezonans v Biologii i Meditsine, Moskva (1989), pp. 82–83 (Russ.).
G. N. Bogdanov, V. N. Varfolomeev, E. E. Morozova, K. A. Treskunov, et al. Blood paramagnetic metallocomplexes and their relation with pathological states, Magnitnyi Rezonans v Biologii i Meditsine, Moskva (1981), pp. 191–192 (Russ.).
M. Bomba, A. Camagna, S. Cannistraro, P. L. Indovina and P. Samoggia, EPR study of serum ceruloplasmin and iron transferrin in myocardial infarction, Physiol. Chem. Phys. 9:175 (1977).
J. A. Green, T. Pocklington, A. A. Dawson, M. Foster, ESR studies on caeruloplasmin and iron transferrin in patients with chronic lymphocytic leukaemia, Br. J. Cancer 41:356 (1980).
K. R. Sedov and R G. Saifutdinov, Electron Paramagnetic Resonance in Internal Diseases Clinics, Irkutskii Dom Pechati, Irkutsk (1993) (Russ.).
L. I. Idel’son, Hipochromic Anemia, Meditsina, Moskva (1981).
V. N. Petrov, Physiology and Pathology of Iron Metabolism, Nauka, Leningrad (1982) (Russ.).
T. V. Golosova, E. M. Vlasikhina and I. N. Pobedinskaya, Serologic markers of viral hepatitis B in hematological patients, Gematologiya itransfuziologiya. N1:7 (1987) (Russ.).
P. D. Howotle, G. M. Wood, S. G. A. Romaskile and M. S. Losowsky, Chronic hepatitis “B” carriers found at blood donation. Do they need regular follow-up? Vox. Sang. 52:200 (1987).
M. S. Kushakovskii, Clinical Forms of Hemoglobin Damage, Meditsina, Leningrad (1968) (Russ.).
M. S. Moxness, L. S. Brunauer and W. H. Huestis, Hemoglobin oxidation products extract phospholipids from the membrane of human erythrocytes, Biochemistry. 35:7181 (1996).
D. A. Svistunenko, R. P. Patel and M. T. Wilson, An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: methods to quantify all paramagnetic species observed in the reaction, Free Radic. Res. 24:269 (1996).
Neto L. Martin, M. Tabak and O. R Nascimento, Effect of hydration in metHb: reversible changes monitored by ESR of iron, J. Inorg. Biochem. 40:309 (1990).
N. Nedjar-Arroume, A. Castellano, J. M. Piot and D. Guillochon, Stabilizing effect of water/alcohol solvents towards autoxidation of human hemoglobin, Biotechnol. Appl. Biochem. 18 (Pt1):25 (1993).
N. Kosover and E. Kosover, Glutathione disulfate systems, in: Free Radicals in Biology, Mir, Moskva (1979), pp. 65–95 (Russ.).
N. P. Skakun and V. I Shendevitskii, Pharmacokinetics of MetHb-forming agents, Terapevt. Arkhiv. N1:100 (1980) (Russ.).
M. Nagai, K. Mawatari, Y. Nagai, S. Horita, Y. Yoneyama and H. Hori, Studies of the oxidation states of hemoglobin M Boston and hemoglobin M Saskatoon in blood by EPR spectroscopy, Biochem. Biochem. Biophys. Res. Commun. 210:483 (1995).
I. B. Afanas’ev, Free radical inhibitors and promotors of biological processes, in: Oxygen Radicals in Chemistry, Biology and Medicine, Zinatne, Riga (1988), pp. 9–25 (Russ.).
G. A. Hamilton and R. D. Libby, The valence of copper and the role of supperoxide in the D-galactoae oxidase catalyzed reaction, Biochem. Biophys. Res. Commun. 55:333 (1973).
A. G. Shanturov, E. V. Nosulya and R. G. Saifutdinov, EPR study of the nasal secretion metalloproteins, Vestnik otorholaringologii. N6: 13 (1991) (Russ.).
E. V. Nosulya, A. G. Shanturov and R. G. Saifutdinov, EPR study of the nasal secretion in normal and upper respiratory tract pathology, Ru Magnitnyi Rezonans v Khimii i Biologii, May 26–June 2, Zvenigorod (1996), p.61 (Russ.).
R. G. Saifutdinov, E. V. Nosulia and A. G. Shanturov, Investigation by ESR of the nose secret received from human, YI International Symposium on Magnetic Resonance in Colloid and Interface science, Ference (1992), p. 177.
M. Machnicki, Biological properties of lactotransferrin, Folia Biol. (Praha). 37:65 (1991).
C. L. Day, K. M. Stowell, E. N. Baker and J. W. Tweedie, Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release, J. Biol. Chem. 267:13857 (1992).
D. Legrand, J. Mazurier, D. Colavizza, J. Montreuil and G. Spik, Properties of the iron-binding site of the N-terminal lobe of human and bovine lactotransferrins. Importance of the glycan moiety and of the non-covalent interactions between the N-and C-terminal lobes in the stability of the iron-binding site, Biochem. J. 266:575 (1990).
R. G. Saifutdinov, Paramagnetic Centers in Human Biological Fluids and Their Diagnostic and Pathogenetic Role in Some Internal Diseases, Thesis Dr. Sci., Medical Institute, Tomsk (1989) (Russ.).
T. M. Lachocki, D. F. Church and W. A. Pryor, Persistent free radicals in the smoke of common household materials: biological and clinical implications, Environ. Res. 45: 127 (1988).
0. Zschornig, H. Machill, O. M. Panasenko, T. V. Volnova, K. Arnold and O. A. Azizova, Influence of polar polymers on the apoprotein region of human serum lipoproteins: an electron paramagnetic resonance (EPR) study, Gen. Physiol. Biophys. 12: 113 (1993).
M. Kveder, G. Pifat, S. Pecar and M. Schara, The ESR characterization of molecular mobility in the lipid surface layer of human serum lipoproteins, Chem. Phys. Lipids. 70: 101 (1994).
M. Kveder, G. Pifat, S. Pecar, M. Schara, P. Ramos and H. Esterbauer, Nitroxide reduction with ascorbic acid in spin labeled human plasma LDL and VLDL, Chem. Phys. Lipids. 85:1 (1997).
H. Lottin, C. Motta and G. Shard, Differential effects of glycero-and sphingo-phospholipolysis on human high-density lipoprotein fluidity, Biochim. Biophys. Acta. 1301:127 (1996).
O. V. Sviridov, M. N. Ermolenko, E. S. Pyshko, S. V. Khalimondhik, N. A. Gurinovich, S. L. Romanov, P. A. Kiselev and 0. A. Strel’chenok, Isolation, identification and properties of a new thyroxine-binding protein-apolipoprotein A-1 from human blood serum, Biokhimiia. 56:2281 (1991) (Russ.).
O. M. Panasenko, T. V. Volnova, 0. A. Azizova, Y. A. Vladimirov, Free radical modification of lipoproteins and cholesterol accumulation in cells upon atherosclerosis, Free Radic. Biol. Med. 10:137 (1991).
C. E Thomas, G. Ku and B. Kalyanaraman, Nitrone spin trap lipophilicity as a determinant for inhibition of low density lipoprotein oxidation and activation of interleukin-1 β release from human monocytes, J. Lipid. Res. 35:610 (1994).
P. K. Witting, J. M. Upston and R. Stocker, Role of α-tocopheroxyl radical in the initiation of lipid peroxidation in human Loe-density lipoprotein exposed to horse radishperoxidase, Biochemistry. 36:1251 (1997).
S. R. Thomas, P. K. Witting and R. Stocker, 3-Hydroxyanthranilic acid is an efficient, cell-derived co-antioxidant for alpha-tocopherol, inhibiting human low density lipoprotein and plasma lipid peroxidation, J. Biol. Chem. 271:32714 (1996).
J. M. Upston, J. Neuzil and R Stocker, Oxidation of LDL by recombinant human 15-lipoxygenase: evidence for α-tocopherol-dependent oxidation of esterified core and surface lipids, J. Lipid Res. 37:2650 (1996).
P. K. Witting, J. M. Upston and R. Stocker, Role of α-tocopheroxyl radical in the initiation of lipid peroxidation in human Loe-density lipoprotein exposed to horse radish peroxidase, Biochemistry. 36:1251 (1997).
V. E. Kagan, E. A. Serbinova, T. Forte, G. Scita and L. Packer, Recycling of vitamin E in human low density lipoproteins, J. Lipid. Res. 33:385 (1992).
M. F. Muldoon, S. B. Kritchevsky, R. W. Evans and V. E. Kagan, Serum total antioxidant activity in relative hypo-and hypercholesterolemia, Free Radic. Res. 25:239 (1996).
O. M Panasenko, S. A. Evgina and V. I. Sergienko, A spin-probe study of the structural change in human blood lipoproteins under the action of sodium hypochlorite, Biull. Eksp. Biol. Med. 116:153 (1993) (Russ.).
O. M. Panasenko, S. A. Evgina, S. V. Nikitin and V. I. Sergienko, The effect of hypochlorite on electrical surface properties of human blood lipoproteins, Biofizika. 40:545 (1995) (Russ.).
C. G. Taylor, M. K. Dame, H. S. Murphy, P. A. Ward and J. Varani, Spontaneous injury to human umbilical vein endothelial cells increases during in vitro culture and is blocked by protein kinase activation, Lab. Invest. 70:822 (1994).
S. L. Hempel, G. R. Buettner, D. A. Wessels, G. M. Galvan and Y. Q. O’Malley, Extracellular iron (II) can protect cells from hydrogen peroxide, Arch. Biochem. Biophys. 330:401 (1996).
V. O’Donnell and M. J. Burkitt, Mitochondrial metabolism of a hydroperoxide to free radicals in human endothelial cells: an electron spin resonance spin-trapping investigation, Biochem. J. 304 (Pt3):707 (1994).
J. Van der Zee, Formation of peroxide-and globin-derived radicals from the reaction of methaemoglobin and metmyoglobin with t-butyl hydroperoxide: an ESR spin-trapping investigation, Biochem. J. 322 (Pt 2):633 (1997).
L. Pronai, K. Hiramatsu, Y. Saigusa and H. Nakazawa, Low superoxide scavenging activity associated with enhanced superoxide generation by monocytes from male hypertriglyceridemia with and without diabetes, Atherosclerosis. 90:39 (1991).
K. R. Sedov and R G. Saifutdinov, Blood and blood components free radicals and their significance in IHD diagnosis, Ru IV Vsecoyunyi S’ezd Kardiologov, Moskva, (1986), pp. 40–41 (Russ.).
K. R. Sedov and R. G. Saifutdinov, Blood free radicals and their value in IHD diagnosis, Bulleten’ Sibirskogo Otdeleniyab AMN SSSR, Novosibirsk, N6:73 (1985) (Russ.).
R. G. Saifutdinov, A study of blood free radicals in myocardial infarction patients, Novye Napravleniya v Kardiologii. Infarkt Miokarda, Nedostatochnost’ Krovoobrashcheniya, Novokunetsk (1987), pp. 46–47 (Russ.).
R. G. Saifutdinov and K. R Sedov, Differential diagnosis of stenocardia from cardiology, Pat SSSR N 1061800 (1982), Bull. Izobr. N47:21 (1983) (Russ.).
I. K. Shvatsabaya, Ischaemic Heart Disease, Meditsina, Moskva (1975) (Russ.).
M. E. Raiskina, The role of catecholamines in cardiac metabolism, in: Biogene Amines, Meditsina, Moskva (1967), pp. 86–102 (Russ.).
R. G. Saifutdinov, Adrenalin effect on free radical levels in humen plasma and erythrocytes, Bulleten’ Eksperimental’noi Biologii i Meditsiny. N10:78 (1982) (Russ.).
A. M. Shaposhnikova and E. F. Derkachev, Ceruloplasmin interaction with cell electron-transporting systems, Biokhimiya. 36:3 (1971) (Russ.).
L. Broman, Chromatographic and magnetic studies on human ceruloplasmin, Acta Soc. Med. Upsal. 69:1 (1964).
T. Kakuda, H. Tanaka, E. Kimoto and F. Morishige, EPR spectrum of human serum copper, Appl. Spectrosc. 34:276 (1980).
A. Mouithys-Mickalad, P. Hans, G. Deby-Duponf M. Hoebeke, C. Deby and M. Lamy, Propofol reacts with peroxynitrite to form a phenoxyl radical: demonstration by electron spin resonance, Biochem. Biophys. Res. Commun. 249:833 (1998).
J. G. Coghlan, W. D. Flitter, A. E. Holley, M. Norell, A. G. Mitchell, C. D. Ilsley and T. F. Slater, Detection of free radicals and cholesterol hydroperoxides in blood taken from the coronary sinus of man during percutaneous transluminal coronary angioplasty, Free. Radic. Res. Commun. 14:409 (1991).
A. J. Tortolani, S. R. Powell, V. Misik, W. B. Weglicki, G. J. Pogo and J. H. Kramer, Detection of alkoxyl and carbon-centered free radicals in coronary sinus blood from patients undergoing elective cardioplegia, Free Radic. Biol. Med. 14:421 (1993).
E. D. Grech, N. J. Dodd, M. J. Jackson, W. L. Morrison, E. B. Faragher, D. R. Ramsdale, Evidence for free radical generation after primary percutaneous transluminal coronary angioplasty recanalization in acute myocardial infarction, Am. J. Cardiol. 77:122 (1996).
J. L. Zweier, R. Broderick and P. Kuppusamy, Determination of the mechanism of free radical generation in human aortic endothelial cells exposed to anoxia and reoxygenation, J. Biol. Chem. 269:24156 (1994).
S. Pietri, J. R. Seguin, P. D. d’Arbigny and M. Culcasi, Ascorbyl free radical: a noninvasive marker of oxidative stress in human open-heart surgery, Free Radic. Biol. Med. 16:523 (1994).
J. L. Zweier, P. Wang, A. Samouilov and P. Kuppusamy, Enzyme-independent formation of nitric oxide in biological tissues [see comments], Nat. Med. 1:804 (1995).
M. Pissarek, F. Janichen, I. E. Blasig, R. Haseloff, T. Keller, E. Tapp and EG. Krause, Cardioprotective potency of the radical scavenger S-2-(3 aminopropylamino) ethylphosphorothioic acid in the post-ischaemic rat heart, Mol. Cell. Biochem. 145: 121 (1995).
A. Movahed, K. G. Nair, T. F. Ashavaid and P. Kumar, Free radical generation and the role of allopurinol as a cardioprotective agent during coronary artery bypass grafting surgery, Can. J. Cardiol. 12: 138 (1996).
K. B. Shumaev, V. Ya. Bykhovskii, V. V. Kukharchuk and E. K. Ruuge, Hydrophobic antioxidant radical forms: possible role in POLL protection, Fizika i Khimiya Elementarnykh Khimicheskikh Protsessov; Ru V Vserossiiskaya Konferentsiya, Posvyashchennaya 80-letiyu Akademika V.V. Voevodskogo, September 29–October 3, Chernogolovka (1997), pp. 296–298 (Russ.).
V. E. Kagan, H. J. Freisleben, M. Tsuchiya, T. Forte and L. Packer, Generation of probucol radicals and their reduction by ascorbate and dihydrolipoic acid in human low density lipoproteins, Free Radic. Res. Commun. 15:265 (1991).
P. Ascenzi, M. Coletta, A. Desideri, R. Petruzzelli, F. Polizio, M. Bolognesi, S. G. Condo and B. Giardina, Spectroscopic properties of the nitric oxide derivative of ferrous man, horse, and ruminant hemoglobins: a comparative study, J. Inorg. Biochem. 45:31 (1992).
P. Ascenzi, M. Coletta, A. Desideri, F. Polizio, A. Bertollini, R. Santucci and G. Amiconi, Effect of bezafibrate and clofibric acid on the spectroscopic properties of the nitric oxide derivative offerrous human hemoglobin, J. Inorg. Biochem. 48:47 (1992).
T. G. Gantchev and M. B. Shopova, Characterization of spin-labelled fatty acids and hematoporphyrin binding sites interactions in serum albumin, Biochim. Biophys. Acta. 1037:422 (1990).
E. P. Sidorik, Yu. B. Bogaev and AP. Burlaka, Instrumental problems in EPR diagnosis of tumors lung diseases, Problemy tekhniki v meditsine, Tomsk (1983), pp. 58–59 (Russ.).
E. I. Chazov, Coronary Insufficiency (Progress in Theoretical and Clinical Cardiology), Meditsina, Moskva, (1977) (Russ.).
N. M. Mukharlyamov, Early Stages of Circulation Deficiency and its Compensatory Mechanism, Meditsina, Moskva, (1978) (Russ.).
L. I. Ol’binskaya and P. F. Litvitskii, Coronary and Myocardic Insufficiency. Meditsina, Moskva (1986) (Russ.).
V. Z. Gorkin, Modern view on contribution of E and K vitamins and related compounds to oxidative phosphorylation, Ukrainskii biokhimicheskii zhurnal. 31:270 (1959) (Russ.).
R. G. Saifutdinov, Effect of α-tocopherole on concentration of α-tocopherylquinone human blood lipids, Bulleten’ Eksperimental’noi Biologii i Meditsiny. N9:296 (1985) (Russ.).
L. R. Cantilena Jr, R. P. Smith, S. Frasur, H. Kruszyna, R. Kruszyna and D. E. Wilcox, Nitric oxide hemoglobin in patients receiving nitroglycerin as detected by electron paramagnetic resonance spectroscopy [see comments], J. Lab. Clin. Med. 120:902 (1992).
H. Kosaka, S. Tanaka, T. Yoshii, E. Kumura, A. Seiyama and T. Shiga, Direct proof of nitric oxide formation from a nitrovasodilator metabolised by erythrocytes, Biochem. Biophys. Res. Commun. 204:1055 (1994).
D. Sh. Burbaev, Paramagnetic Iron-Serum Center in Electron Transport Chain of Membrane Biological Structure, Thesis Dr.Sci., Moskva (1986) (Russ.).
M. M. Muratov, Formaldehyde Effect on the Electron Transport Chain of Heart Conserved Mitochondria. Thesis Ph.D., Kazan (1981) (Russ.).
K. R. Sedov and R G. Saifutdinov, EPR posibility in circular deficience patients, Novye Napravleniya v Kardiologii. Infarkt Miokarda, Nedostatochnost’ Krovoobrashcheniya, Novokunetsk (1987), pp. 11–12 (Russ.).
A. M Komarov and C. S. Lai, Detection of nitric oxide production in mice by spin-trapping electron paramagnetic resonance spectroscopy, Biochim. Biophys. Acta. 1272:29 (1995).
V. Quaresima, H. Takehara, K. Tsushima, M. Ferrari and H. Utsumi, In vivo detection of mouse liver nitric oxide generation by spin trapping electron paramagnetic resonance spectroscopy, Biochem. Biophys. Res. Commun. 221:729 (1996).
S. Al-Dabbagh and R. Dolt, N-nitroso compounds: occurence, biological effects and relevance to human cancer, (IARC Sci. Publ. N57), Lyon (1983), pp. 901–909
R. G. Saifutdinov and A. V. Sukhanov, Study of nitrate-reducing ability of saliva Magnetic resonance and related phenomena, XXVII-th Congress Ampere, August 21–28, Kazan (1994), pp. 910–911.
R. G. Saifutdinov and A. V. Sukhanov, The nitrate-reducing ability of the saliva, XYI International Conference on Magnetic Resonance in Biological Systems (ISMRBS), The Netherlands, Veldhoven, (1994).
A. V. Sukhanov, Biological Fluid Nitrate-Reducing Capability in Some Internal Diseases, Thesis Ph.D., Institut Usovershenstvovaniya Vrachei, Irkutsk (1999) (Russ.).
R. G. Saifutdinov and A. V. Sukhanov, Nitrate-reducing ability of saliva, International Conference EPR-spectroscopy of nitric oxide in biological systems, December 11–15, Suzdal (1996), pp. 27–28.
A. E. Kalmanson, On the Nature and Role of Free Radicals in Biological Processes, Thesis Ph.D., Institute of Chem. Phys, Moskva (1977) (Russ.).
A. E. Kalmanson, A. V. Belozerova and N. S. Motavkina, EPR spectra of intestinal and coccal group pathogenes, Ru IV Mezhdunarodnyi Biofizicheskii Kongress, Moskva (1972), V. 4, pp. 220–221 (Russ.).
R. G. Saifutdinov, K. V. Protasov and V. S. Kustos, Intestinal microflora PMCs in IHD patients taking dairy products, Ru Magnitnyi Rezonans v Khimii i Biologii, May 26–June 2, Zvenigorod (1996), pp. 69–70 (Russ.).
R. G. Saifutdinov, V. S. Kustos and K. V. Protasov, Investigation offaeces by EPR/ESR at patients with coronary heart deasease, taking sour milk products, 2eme Symposium Satellite “Vitamins and Biofactors”, September 27–28, France, Nancy (1996).
G. G. Kuznetsova, Intestinal biocenosis disorders in chronic colites, Sov. Meditsina N11:62 (1972) (Russ.).
A. I. Oparin, E. F. Kharat’yan and N. S. Gel’man, Dehydrogenase localisation and relation to lactobacterium pentoaceticum cellular oxygen, Dokl. Mad. Nauk SSSR. 64:211 (1964) (Russ.).
E. A. Boichenko and A. I. Oparin, Metal compounds interaction in hydrogenase evolution, Zhumal evolyutsionnoi biokhimii. 16:3 (1980).
E. W. Ainscough and A. M. Brodie, ESR spectrometry and its application to biochemistry, Chem. N. Z. 47:86 (1983).
K. V. Protasov, Holesterin-Transfering Ability of MD Patient Intestal Microflora, Institut Usovershenstvovaniya Vrachei, Irkutsk (1998) (Russ.).
M. Persson, P. Hammarstrum, M. Lindgren, B. H. Jonsson, M. Svensson and U. Carlsson, EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction, Biochemistry. 38(1):432 (1999).
L. A. Wheeler, F. B. Soderberg and P. Goldman, The relationship between nitro group reduction and the intestinal microflora, J. Pharmacol. Exp. Ther. 194:135 (1975).
Ya I. Azhipa, Medical-Biological Aspects of Electron Paramagnetic Resonance Applications, Nauka, Moskva (1983) (Russ.).
S. L. Gorbach and E. Bengt Gustafsson memorial lecture. Function of the normal human microflora, Scand. J. Infect. Dis. Suppl. 49:17 (1986).
A. L. Myasnikov, Hypertension Disease and Atherosclerosis, Meditsina, Moskva (1965) (Russ.).
B. M. Braginskii, M. A. Lis and V. P. Vodoevich, Thiamine sufficiency in patients with hypertensive diseases and atherosclerosis, Zdravookhranenie Belorussii. N8:26 (1972) (Russ.).
Yu. V. Zobnin, Blood PMCs and Lipid Free Radicals Oxidation in the Baikal-Amur Railway Road Builders with Arterial Hypertension, Thesis Ph.D., Cardiology Institute, Tomsk (1986) (Russ.).
A. L. Kleshchev, Nitric Oxide as a General Metabolite of Nitrogen-Containing Vasodilators and Guanylacyclase Activators. Hypertensive properties of free and iron-bonding NO, Thesis Ph.D., 1st Medical Institute, Moskva (1986) (Russ.).
J. R. Stone, R H. Sands, W. R. Dunham and M. A. Marletta, Electron paramagnetic resonance spectral evidence for the formation of a pentacoordinate nitrosyl-heme complex on soluble guanylate cyclase, Biochem. Biophys. Res. Commun. 207:572 (1995).
P. F. Chen, A. L. Tsai, V. Berka and K. K. Wu, Mutation of Glu-361 in human endothe-lial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers, J. Biol. Chem. 272:6114 (1997).
A. K. Nussler, D. A. Geller, M. A. Sweetland, M. Di Silvio, T. R. Billiar, J. B. Madariaga, R. L. Simmons and J. R. Lancaster Jr., Induction of nitric oxide synthesis and its reactions in cultured human and rat hepatocytes stimulated with cytokines plus LPS, Biochem. Biophys. Res. Commun. 194:826 (1993).
J. Vasquez-Vivar, A. M. Santos, V. B. Junqueira and O. Augusto, Peroxynitrite-mediated formation of free radicals in human plasma: EPR detection of ascorbyl, albumin-thiyl and uric acid-derived free radicals, Biochem. J. 314 (Pt3):869 (1996).
R. B. Clarkson, S. W. Norby, A. Smirnov, S. Boyer, N. Vahidi, R. W. Nims and D. A. Wink, Direct measurement of the accumulation and mitochondrial conversion of nitric oxide within Chinese hamster ovary cells using an intracellular electron paramagnetic resonance technique, Biochim. Biophys. Acta. 1243:496 (1995).
A Wennmalm, G Benthin, A Edlund, N Kieler-Jensen, S Lundin, AS Peterson and F. Waagstein, Nitric oxide synthesis and metabolism in man, Ann. N.-Y. Acad. Sci. 714:158 (1994).
T. Yamamura, Techniques for measurement of nitric oxide in biological systems: principles and practice, Nippon Yakurigaku Zasshi. 107:173 (1996).
A. Wennmalm, B. Lanne and A. S. Petersson, Detection of endothelial-derived relaxing factor in human plasma in the basal state and following ischemia using ESR spectrometry, Anal. Biochem. 187:359 (1990).
G. G. Borisenko, A. N. Osipov, K. D. Kazarinov and Yu. A. Vladimirov, Photochemical reactions of nitrosyl hemoglobin during exposure to low-power laser irradiation, Biokhimiay. 62:661 (1997) (Russ.).
H. Kruszyna, R. Kruszyna, L. G. Rochelle, R. P. Smith and D. E. Wilcox, Effects of temperature, oxygen, heme ligands and sulfhydryl alkylation on the reactions of nitroprusside and nitroglycerin with hemoglobin, Biochem. Pharmacol. 46:95 (1993).
D. N. Rao, S. Elguindi and P. J. O’Brien, Reductive metabolism of nitroprusside in rat hepatocytes and human erythrocytes, Arch. Biochem. Biophys. 286:30 (1991).
D. Pietraforte and M. Minetti, One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centredradicals, Biochem. J. 321 (Pt 3):743 (1997).
M. R. Gunther, L. C. Hsi, J. F. Curtis, J. K. Gieras, L. J. Marnett, T. E. Eling and R. P. Mason, Nitric oxide trapping of the tyrosyl radical of prostaglandin H synthase-2 leads to tyrosine iminoxyl radical and nitrotyrosine formation, J. Biol. Chem. 272: 17086 (1997).
M. Minetti, G. Scorza and D. Pietraforte, Peroxynitrite induces long-lived tyrosyl radical(s) in oxyhemoglobin of red blood cells through a reaction involving CO2 and a ferryl species, Biochemistry. 38:2078 (1999).
H. Kosaka and A. Seiyama, Physiological role of nitric oxide as an enhancer of oxygen transfer from erythrocytes to tissues, Biochem. Biophys. Res. Commun. 218:749 (1996).
M. B. Johnson, J. G. Adamson and A. G. Mauk, Functional comparison of specifically cross-linked hemoglobins biased toward the R and T states, Biophys. J. 75:3078 (1998).
M. F. R. Martin, K. E. Surrall, F. McKenna, J. S. Dixon, H. A. Bud and V. Wright., Captopril: a new treatment for rheumatoid arthritis, Lancet. 1:1325 (1984).
W. H. van Gilst, P. A. de Graeff, H. Wesseling and C. D. J. de Langen, Reduction of reperfusion arrhythmia in the ischemic isolated rat heart by angiotensin cinverting enzyme inhibitors: A comparison of captopril, enalapril and HOE 498, J. Cardiovascular Pharmacol. 8:722 (1986).
V. Misik, I. T. Mak, R. E. Stafford and W. B. Weglicki, Reactions of captopril and epicaptopril with trandition metal ions and OH radicals-an EPR spectroscopy study, Free Radic. Biol. Med. 15:611 (1993).
D. Bagchi, R. Prasad and D. K. Das, Direct scavenging of free radicals by captopril an angiotensin converting enzyme inhibitor, Biochem. Biophys. Res. Comm. 158:52 (1989).
O. I. Aruoma, D. Akanmu, R. Cecchini and B. Halliwell, Evaluation of the ability of the angiotensin-converting enzyme inhibitor captopril to scavenge reactive oxygen species, Chem.-Biol. Interact. 77:303 (1991).
D. Jay, A. Cuellar, E. G. Jay, C. Garcia, R. Gleason and E. Munoz, Study of a Fenton type reaction: effect of captopril and chelating reagents, Arch. Biochem. Biophys. 298:740 (1992).
J. Reguli and V. Misik, Superoxide scavenging by thiol/copper complex of captoprilan EPR spectroscopy study, Free Radic. Res. 22:123 (1995).
D. Jay, A. Cuellar, R. Zamorano, E. Munoz and R. Gleason, Captopril does not scavenge superoxide: captopril prevents O2-. production by chelating copper, Arch. Biochem. Biophys. 290:463 (1991).
A. Stasko, V. Brezova, S. Biskupic, K. Ondrias and V. Misik, Reactive radical intermediates formed from illuminated nifedipine, Free Radic. Biol. Med. 17:545 (1994).
C. Dragu, L. Copaescu and V. V. Morariu, Manganese transport through human erythrocyte membranes. An EPR study, Biochim. Biophys. Acta 1328:90 (1997).
J. N. Cohn, S. M. Ziesche, L. E. Loss and G. T. Anderson, Effect of felodipine on short-term exercise and neurohormones and long-term mortality in heart failure: Results of V-HeFT III Circulation. 92 (Suppl 1):1 (1995).
C. M. O’Connor, R. N. Belkin, P. E. Carson, et al., For the PRAISW investigators. Effect of amlodipine on mode of death in severe chronic heart failure, The PRAISW trial (Abstr), Circulation. 92 (Suppl 1):l (1995).
K. Tsuda, Y. Minatogawa, H. Iwahashi, I. Nishio, R Kido and H. Masuyama, Spinlabelling study of biomembranes in spontaneously hypertensive rats: calcium-and calmodulin-dependentregulation, Clin. Exp. Pharmacol. Physiol. 22 (Suppl 1):S234 (1995).
R. G. Saifutdinov and O. N. Koshchina, Blood PMCs in iron-deficient anemic patients before and after treatment by iron-containing medicines, Environment and Human Health (Regional Meeting), Irkutsk Medical Institute, Irkutsk (1990), v. 3, pp. 406–411 (Russ.).
Y. Chen-Barrett, P. M. Harrison, A. Treffry, M. A. Quail, P. Arosio, P. Santambrogio and N. D. Chasteen, Ty-rosyl radical formation during the oxidative deposition of iron in human apoferritin, Biochemistry. 34:7847 (1995).
B. R. Crouse, V. M. Sellers, M. G. Finnegan, H. A. Dailey and M. K. Johnson, Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster, Biochemistry. 35:16222 (1996).
R. G. Saifutdinov, The Possibility of ESR method in clinical medicine, XXVII-th Congress Ampere, August 21–28, Kazan (1994), pp. 908–909.
P. L. Indovina, ESR studies on different pathological states, Ann. 1st. Super. Sanita. 14:863 (1978).
0. B. Priima, Non-enzymatic cation proteins of peripheral blood leukocytes as a factor of nonspecific response of living organism to injury, Klinicheskaya meditsina. N2:4 (1997) (Russ.).
V. E. Pigarevskii, Clinical Morphology of Neutrophilic Granulocytes, Meditsina, Moskva (1988) (Russ.).
B. S. Nagoev, Neutrophilic Granulocytosis, Nal’chik (1986) (Russ.).
W. Chamulitrat, M. S. Cohen and R. P. Mason, Free radical formation from organic hydroperoxides in isolated human polymorphonuclear neutrophils, Free Radic. Biol. Med. 11:439 (1991).
C. E. Cooper and E. Odell, Interaction of human myeloperoxidase with nitrite, FEBS Lett. 314:58 (1992).
C. E. Cooper and E. Odell, EPR differences between human myeloperoxidase isoenzymes, Biochem. Soc. Trans. 20:108S (1992).
B. E. Britigan, T. J. Coffman and G. R. Buettner, Spin trapping evidence for the lack of significant hydroxyl radical production during the respiration burst of human phagocytes using a spin adduct resistant to superoxide-mediateddestruction, J. Biol. Chem. 265:2650 (1990).
C. L. Ramos, S. Pou, B. E. Britigan, M. S. Cohen and G. M. Rosen, Spin trapping evidence for myeloperoxidase-dependent hydroxyl radical formation by human neutrophils and monocytes, J. Biol. Chem. 267:8307 (1992).
V. R. Muzykantov, T. A. Kushnareva, M. D. Smimov and E. K. Ruuge, Avidin attachment to biotinylated human neutrophils induces generation of superoxide anion, Biochim. Biophys. Acta. 1177:229 (1993).
M. L. McCormick, T. L. Roeder, M. A. Railsback and B. E. Britigan, Eosinophil peroxidase-dependent hydroxyl radical generation by human eosinophils, J. Biol. Chem. 269:27914 (1994).
T. R. Green, J. H. Fellman, A. L. Eicher and K. L. Pratt, Antioxidant role and subcellular location of hypotaurine and taurine in human neutrophils, Biochim. Biophys. Acta. 1073:91 (1991).
D. Constantin, K. Mehrotra, B. Jernstrom, A. Tomasi and P. Moldeus, Alternative pathways of sulfite oxidation in human polymorphonuclear leukocytes, Pharmacol. Toxicol. 74:136 (1994).
D. Pietraforte, E. Tritarelli, U. Testa and M. Minetti, gp120 HIV envelope glycoprotein increases the production of nitric oxide in human monocyte-derived macrophages, J. Leukoc. Biol. 55: 175 (1994).
K. Hajela, R.. Kayestha and J. Sumati, Carbohydrate induced modulation of cell membrane. IV: Interaction with mucin and fucoidan totally immobilizes the human platelet membrane, Indian. J. Biochem. Biophys. 33:308 (19%).
K. Hajela, R. Kayestha and J. Sumati, Carbohydrate induced modulation of cell membrane: 11. Spin label study of fluidity changes in peripheral blood lymphocyte membrane, FEBS Lett. 380: 165 (1996).
K. Hajela, R Kayestha and J. Sumati, Carbohydrate induced modulation of cell membrane. V: ESR characterization of molecular mobility in lipid bilayer of human neutrophil plasma membrane, Indian. J. Exp. Biol. 34:513 (19%).
B. Meier, H. H. Radeke, S. Selle, G. G. Habermehl, K. Resch and H. Sies, Human fibroblasts release low amounts of reactive oxygen species in response to the potent phagocyt estimulants, serum-treatedzymosan, N-formyl-methionyl-leucyl-phenylalanine, leukotriene B4 or 12-O-tetradecanoylphorbol 13-acetate, Biol. Chem. Hoppe Seyler. 371: 1021 (1990).
C. D. Black, A. Samuni, J. A. Cook, C. M. Krishna, D. C. Kaufman, H. L. Malech and A. Russo, Kinetics of superoxide production by stimulated neutrophils, Arch. Biochem. Biophys. 286:126 (1991).
D. K. Perry, W. L. Hand, D. E. Edmondson and J. D. Lambeth, Role of phospholipase D-derived diradylglycerol in the activation of the human neutrophil respiratory burst oxidase. Inhibition byphosphatidic acid phosphohydrolase inhibitors, J. Immunol. 149:2749 (1992).
B. M. Babior, Oxidants from phagocytes: agents of defense and destruction, Blood. 64:959 (1984).
B. 0. Anderson, J. M. Brown, A. H. Harken, Mechanisms of neutrophil-mediates tissue injury, J. Surgical. Res. 51:170 (1991).
J. Reguli, Z. Durackova, J. Pogady, D. Martisova and A. Stasko, EPR spin trapping of reactive oxygen products of the respiratory burst of phagocytes (use of EPR spectroscopy in biology and medicine II), Bratisl. Lek. Listy. 93:557 (1992).
L. Seawright, M. Tanigawa, T. Tanigawa, Y. Kotake and E. G. Janzen, Can spin trapping compounds like PBN protect against self-inflicted damage in polymorphonuclear leukocytes?, Free Radic. Res. 23:73 (1995).
Y. Mao, L. Zang and X. Shi, Singlet oxygen generation in the superoxide reaction, Biochem. Mol. Biol. Int. 36:227 (1995).
T. Tanigawa, Y. Kotake, M. Tanigawa and L. A. Reinke, Mutual contact of adherent polymorphonuclear leukocytes inhibits their generation of superoxide, Free Radic. Res. 22:361 (1995).
C. Opper, C. Fett, B. Capito, S. Raha and W. Wesemann, Plasma membrane properties in heterogeneous human blood platelet subfractions modulate the cellular response at the second messenger level, Thromb. Res. 72:39 (1993).
P. Gaffet, F. Basse and A. Bienvenue, Loss of phospholipid asymmetry in human platelet plasma membrane after 1–12 days of storage. An ESR study, Eur. J. Biochem. 222:1033 (1994).
Y. Bayon, M. Croset, D. Daveloose, F. Guerbette, V. Chirouze, J. Viret, J. C. Kader and M. Lagarde, Effect of specific phospholipid molecular species incorporated in human platelet membranes on thromboxane A2/prostaglandin H2 receptors, J. Lipid. Res. 36:47 (1995).
Y. Bayon, M. Croset, F. Guerbette, D. Daveloose, V. Chirouze, J. Viret, J. C. Kader and M. Lagarde, Selective modifications of the phospholipid fatty acid composition in human platelet membranes using nonspecific and specific lipid transfer proteins, Anal. Biochem. 230:75 (1995).
L. Pronai, K. Ichimori, H. Nozaki, H. Nakazawa, H. Okino, A. J. Carmichael and C. M. Arroyo, Investigation of the existence and biological role of L-arginine/nitric oxide pathway in human platelets by spin-trapping/EPR studies, Eur. J. Biochem. 202:923 (1991).
Z. Y. Wen, Z. Y. Yan, T. Gao, H. Dou, J. Lu, D. Sun and Z. Lu, A study of effects of WGA and ConA on RBC membrane receptors using a new ektacytometric method, Clin. Hemorheol. Microcirc. 17:467 (1997).
L. Iuliano, F. Violi, J. Z. Pedersen, D. Pratico, G. Rotilio and F. Balsano, Free radical-mediated platelet activation by hemoglobin released from red blood cells, Arch. Biochem. Biophys. 299:220 (1992).
L. Iuliano, J. Z. Pedersen, D. Pratico, G. Rotilio and F. Violi, Role of hydroxyl radicals in the activation of human platelets, Eur. J. Biochem. 221:695 (1994).
C. Watala, T. Pietrucha, K. Gwozdzinski, U. Kralisz and C. S. Cierniewski, Microenviron-ment changesinhuman blood platelet membranes associated with binding of tissue-type plasminogen activator, Eur. J. Biochem. 215:867 (1993).
T. Pietrucha, W. J. Stec, A. Okruszek, B. Uznanski, M. Kozio Ekiewicz, A. Wilk, A. Peucienniczak, M. Swiatkowska and C. S. Cierniewski, The epidermal growth factor-like domain from tissue plasminogen activator. Cloning in E. coli, purification and ESR studies of its interaction with human blood platelets, Acta Biochim. Pol. 41:25 (1994).
V. L. Nienaber and L. J. Berliner, Subtle differences in active site structure between bovine and human thrombins: ESR and fluorescence studies, Thromb. Haemost. 65:40 (1991).
L. J. Berliner and J. K. Woodford, Biophysical studies of interactions of hirudin analogs with bovine and human thrombin by ESR and fluorescence labelling studies, Adv. Exp. Med. Biol. 340:51 (1993).
R. O. Hynes, Fibronectins, Springer-Verlag, New York (1990).
C. Narasimhan and C. S. Lai, Differential behavior of the two free sulfhydryl groups of human plasma fibronectin: effects of environmental factors, Biopolymers. 31:1159 (1991).
S. Suzuki, K. Sugai, H. Sato, M. Sakatume and M. Arakawa, Inhibition of active oxygen generation by dipyridamole in human polymorphonuclear leukocytes, Eur. J. Pharmacol. 227:395 (1992).
C. Watala and K. Gwozdzinski, Effect of aspirin on conformation and dynamics of membrane proteins in platelets and erythrocytes, Biochem. Pharmacol. 45:1343 (1993).
Y. Sato, T. Miura and Y. Suzuki, Interaction of pentoxifylline with human erythrocytes. II. Effects of pentoxifylline on the erythrocyte membrane, Chem. Pharm. Bull. (Tokyo). 38:555 (1990).
S. Suzuki, K. Sugai, H. Sato and M. Arakawa, Effect of a platelet-activating factor antagonist, WEB 2086, on inhibition of active oxygen generation in human polymorphonuclear leukocytes, Pharmacology. 48:111 (1994).
G. I. Dorofeev and V. M. Uspenskaya, Gastroduodenal Diseases in Young Age, Meditsina, Moskva (1984) (Russ.).
V. G. Podoprigorova, LPO disorder and antioxidant system state as a partial mechanism in ulceric disease, Ru XIX Vsesoyuznyi S’ezd Terapevtov, Tashkent (1987), V. 2, pp. 349–360 (Russ.).
V. Kh. Vasilenko, A. L Grebnev and A. A. Sheptulin, Ulcer Disease, Meditsina, Moskva (1987) (Russ.).
D. J. Pountney, J. K. Shergill, R J. Simpson and J. M. Wrigglesworth, EPR and visible spectroscopic analysis of a duodenal b-type cytochrome implicated in the process of intestinal iron absorption, Biochem. Soc. Trans. 23:140S (1995).
R. G. Saifutdinov, I. L. Petrunjko, M. B. Shapochnik and S. P. Chicoteev, Investigation of gastric Mucosa by EPR, YII International Symposium on Magnetic Resonance in Colloid and Interface (ISMRCIS YII), Spain, Madrid (1995).
K. R. Sedov and R G. Saifutdinov, Method EPR in clinical medicine, The II-nd International Symposium of Japan-Russia Medical Exchange Foundation and the Hear Region, Vladivostok (1994), p. 289.
J. B. Hibbs, B. R. Taintor, Z. Vavrin, D. L. Granger, J. C. Drapier, I. J. Amber and J. R. Lancaster, Synthesis of nitric oxide from a terminal guanidino nitrogen atom of L-arginine: a molecular mechanism regulating cellular proliferation that targets itracellular iron, in: Nitric Oxide from L-Arginine: a Bioregulatory System, S. Moncada, E. A. Higgs, eds., Elsevier Science Publishers B.V. (Biochemical Division), (1990), pp. 159–223.
A. Wennmalm, B. Lanne and A. S. Petersson, Detection of endothelial-derived relaxing factor in human plasma in the basal state and following ischemia using electron paramagnetic resonance spectrometry, Analytical Biochem. 187:359 (1990).
V. P. Kryshen’ and M. F. Nesterova, Food channel microbial flora in gastric and duodenal ulcer, Vracheb delo. N9:16 (1982) (Russ.).
H. M. Swartz and T. Walczak, In vivo EPR: prospects for the 90s., Phys. Med. 9:41 (1993).
G. R. Eaton, S. S. Eaton and K. Ohno, eds., EPR Imaging and In-vitro EPR, CRC Press, FL, Boca Raton (1991).
V. V. Khramtsov, L. M. Vainer, V. A. Rar, T. A. Berezina, V. V. Martin and L. B. Volodarskii, Macromolecular spin pH-probes on the basis of human serum albumin, Biokhimiya. 55:1014 (1990) (Russ.).
B. Gallez, K. Mader and H. M. Swartz, Noninvasive measurement of the pH inside the gut by using pH-sensitive nitroxides. An in vivo EPR study, Magn. Reson. Med. 36:694 (1996).
T. Ohara, R. Sasaki, D. Shibuya, S. Asaki and T. Toyota, Effect of omeprazole on ascorbate free radical formation, Tohoku J. Exp. Med. 167:185 (1992).
T. Yoshikawa, Y. Naito, T. Tanigawa and M. Kondo, Free radical scavenging activity of the novel anti-ulcer agent rebamipide studied by electron spin resonance, Arzneimittelforsch. 43:363 (1993).
N. Yoshida, T. Yoshikawa, S. Iinuma, M. Arai, S. Takenaka, K. Sakamoto, T. Miyajima, Y. Nakamura, N. Yagi, Y. Naito, F. Mukai and M. Kondo, Rebamipide protects against activation of neutrophils by Helicobacter pylori, Dig. Dis. Sci. 41:1139 (1996).
I. M. Drake, M. J. Davies, N. P. Mapstone, M. F. Dixon, C. J. Schorah, K. L. White, D. M. Chalmers and A. T. Axon, Ascorbic acid may protect against human gastric cancer by scavenging mucosal oxygen radicals, Carcinogenesis. 7:559 (1996).
L. Pronai, I. Yukinobu, I. Lang and J. Feher, The oxygen-centered radicals scavenging activity of sulfasalazine and its metabolites. A direct protection of the bowel, Acta Physiol. Hung. 80:317 (1992).
J. Hargreaves, Y. Popineau, M. Le Meste and M. A. Hemminga Molecular flexibility in wheat gluten proteins submitted to heating, FEBS Lett. 372:103 (1995).
J. Hargreaves, Y. Popineau, M. Cornec and J. Lefebvre, Relations between aggregative, viscoelastic and molecular properties in gluten from genetic variants of bread wheat, Int. J. Biol. Macromol. 18:69 (1996).
H. M. Swartz, K. Chen and J. A. Roth, Further evidence that the pigment in the Dubin-Johnston syndrome is not melanin, Pigment Cell Res. 1:69 (1987).
K. Keddad, P. Therond, C. Motta, C. Baussan and A. Legrand, Alterations in erythrocyte membrane fluidity and fatty acid composition in glycogen storage disease, Biochim. Biophys. Acta. 1315:61 (1996).
G. P. Butcher, A. Raqabah, M. J. Jackson, J. Hoffman, J. M. Rhodes and M. C. Symons, Failure of electron paramagnetic resonance spectroscopy studies to detect elevated free radical signals in liver biopsy specimens from patients with alcoholic liver disease, Free Radic. Res. 22:99 (1995).
P. Clot, G. Bellomo, M. Tabone, et al., Detection of antibodies against proteins modified by hydroxyethyl free radicals in patients with alcoholic cirrhosis, Gastroent. 108:201 (1995).
D. N. Rao, M. X. Yang, J. M. Lasker and A. I. Cederbaum, 1-Hydroxyethyl radical formation during NADPH-and NADH-dependent oxidation of ethanol by human liver microsomes, Mol. Pharmacol. 49:814 (1996).
A. Icen, Glutathione reductase of human erythroeytes, Scand. J. Clin. Invest. 96:1 (1967).
L. Chruscinski, M. Dyba, M. Jezowska-Bojczuk, Henryk-Kozwski, G. Kupryszewski, Z. Mackiewicz and A. Majewska, Specific interactions of Cu2+ ions with fragments of envelope protein of hepatitis B virus, J. Inorg. Biochem. 63:49 (1996).
T. Matsuo, H. Shinzawa, H. Togashi, M. Aoki, K. Sugahara, K. Saito, T. Saito, T. Takahashi, I. Yamaguchi, M. Aoyama and H. Kamada, Free Radic. Biol. Med. 25:929 (1998).
J. Sun, T. M. Loehr, A. Wilks and P. R. Ortiz de Montellano, Identification of histidine 25 as the heme ligand in human liver heme oxygenase, Biochemistry. 33:13734 (1994).
L. H. Patterson, S. Jones and A. Gescher, Generation of a free radical from calphostin C by microsomal cytochrome P450 reductase in rat and human liver, Biochem. Pharmacol. 51:599 (1996).
Y. Dai, J. Rashba-Step and A. I. Cederbaum, Stable expression of human cytochrome P4502E1 in HepG2 cells: characterization of catalytic activities and production of reactive oxygen intermediates, Biochemistry. 32:6928 (1993).
A. Berson, C. Wolf, C. Chachaty, C. Fisch, D. Fau, D. Eugene, J. Loeper, J. C. Gauthier, P. Beaune, D. Pompon, P. Maurel and D. Pessayre, Metabolic activation of the nitroaromatic antiandrogen flutamide by rat and human cytochromes P-450, including forms belonging to the 3A and 1A subfamilies, J. Pharmacol. Exp. Ther. 265:366 (1993).
S. Baron, D. Coppenhaver, F. Dianzani, et al., Interferon principles and medical applications, Gavelstone (1992), pp. 47–64.
L. M. Pfeffer and F. R. Landsberger, Interferon-alpha modulates the plasma membrane-cytoskeletal complex of human lymphoblastoid cells sensitive to the antiproliferative action of interferon-alpha, J. Interferon. Res. 10:91 (1990).
A. Aszalos, P. M. Grimley, E. Balint, K. C. Chadha and J. L. Ambrus, On the mechanism of action of interferons: interaction with nonsteroidal anti-inflammatory agents, pentoxifylline (Trental) and cGMP inducers, J. Med. 22:255 (1991).
A. E. Medlock and H. A. Dailey, Human coproporphyrinogen oxidase is not a metalloprotein, J. Biol. Chem. 271:32507 (1996).
Z. H. Yang, K. Wang and X. T. Liu, Studies of electron spin resonance on bilirubin free radicals, Sci. China. 35B: 1093 (1992).
L. X. Chen, J. F. Lu and K. Wang, The influence of bilirubin on fluidity and rotational correlation times of human erythrocyte membrane, Cell Biol. Int. Rep. 16:567 (1992).
B. Commoner, J. L. Townsend and G. Pake, Free radicals in biological materials, Nature. 174:689 (1954).
R. G. Saifutdinov and A. V. Shcherbakova, EPR study of bile cholecystitis patients, Ru Magnitnyi Rezonans v Khimii i Biologii; May 26–June 2, Zvenigorod (1996), p. 72 (Russ.).
A. V. Shcherbakova, Biological Media PMCs in Cholecystitic Patients, Thesis Ph.D., Medical University, Irkutsk (1997) (Russ.).
C. A. Hubel, A. V. Kozlov, V. E. Kagan, R. W. Evans, S. T. Davidge, M. K. McLaughlin and J. M. Roberts, Decreased transferrin and increased transferrin saturation in sera of women with preeclampsia: implications for oxidative stress, Am. J. Obstet. Gynecol. 175 (Pt1):692 (1996).
B. Kalyanarman, C. C. Felix and R. C. Sealy, Semiquinone anion radicals of catechol (amine)s, catechol estrogens, and their metal ion complexes, Environ. Health. Perspectives. 64:185 (1985).
B. M. Mullock and L. J. Shaw, Sources of proteins in human bile, Gut. 26:500 (1985).
A. V. Sherbakova and R. G. Saifutdinov, Human bile study by EPR method, YII International Symposium on Magnetic Resonance in Colloid and Interface (ISMRCIS YII), Spain, Madrid (1995), ref. 188.
G. H. Reed, EPR Studies of Mn (II) Complexes with enzymes and substrates, Biochem. Soc. Trans. 13:567 (1985).
R. G. Saifutdinov and A. V. Sherbakova, The problem of the human protein containing cuprum, 2nd Winter Research Conferences, January 22–27, France, Les Deux Alpes (1995), poster n. 4.
R. G. Saifutdinov and A. V. Sherbakova, Examination of Cu2+ and Fe3+ in blood and bile by EPR method (EPR/ESR) in diagnostics of the cholecystitis, 5th International Meeting on Trace Elements in Medicine and Biology, February 4–7, France, Meribel (1996), p. 163.
A. V. Shcherbakova, R. G. Saifutdinov, Blood EPR study of cholecystitis patients, Ru Magnitnyi Rezonans v Khimii i Biologii, May 26–June 2, Zvenigorod (1996), p. 71 (Russ.).
I. T. Lott, R. Dipaolo, S. S. Raghavan, P. Clopath, Y. A. Milunsky, W. C. Robertson and J.N. Kanfer, Abnormal copper metabolism in Menke’s steely-hair syndrome, Pediat. Res. 13:845 (1979).
M. Lejoyeux, M. P. Bouvard, J. Viret, D. Daveloose, J. Ades and M. Dugas, Modifications of erythrocyte membrane fluidity from patients with anorexia nervosa before and atter refeeding, Psychiatry Res. 59:255 (1996).
K. R. Sedov, A. F. Kolpakova and N. G. Maksimov, Blood PMC of nonspecific chronic lung disease patients, Ru 2 Vsesoyuznyi Kongress po Boleznyam Organov Dykhaniya, September 16–19, Chelyabinsk (1991), p. 85 (Russ.).
S. A. Baglushkin, R G. Saifutdinov and T. P. Sizykh, Plasma PMC of bronchial asthma patients, Diagnostika i Lechenie Tuberkuleza v Novykh Epidemiologicheskikh Usloviyakh, Ulan-Ude (1992), pp. 10–14 (Russ.).
V. Vallyathan and X. Shi, The role of oxygen free radicals in occupational and environmental lung diseases, Environ Health Perspectives. 105 (Suppl 1): 165 (1997).
S. Pinamonti, M. Leis, A. Barbieri, D. Leoni, M. Muzzoli, S. Sostero, M. C. Chicca, A. Carrieri, F. Ravenna, L. M. Fabbri and A. Ciaccia, Detection of xanthine oxidase activity products by EPR and HPLC in bronchoalveolar lavage fluid from patients with chronic obstructive pulmonary disease, Free Radic. Biol. Med. 25:771 (1998).
N. S. Dalal, J. Newman, D. Pack, S. Leonard and V. Vallyathan, Hydroxyl radical generation by coal mine dust: possible implication to coal workers’ pneumoconiosis (CWP), Free Radic. Biol. Med. 18:11 (1995).
N. S. Dalal, B. Jafari, M. Petersen, F. H. Green and V. Vallyathan, Presence of stable coal radicals in autopsied coal miners’ lungs and its possible correlation to coal workers’ pneumoconiosis, Arch. Environ. Health. 46:366 (1991).
H. J. H. Fenton, Oxidation of tartaric acid in presence of iron, J. Chem. Soc. 65:899 (1994).
X. Shi, Y. Mao, L. N. Daniel, U. Saffiotti, N. S. Dalal and V. Vallyathan, Silica radical-induced DNA damage and lipid peroxidation, Environ. Health Perspectives. 102(Suppl 10): 149 (1994).
V. Vallyathan, J. F. Mega, X. Shi and N. S. Dalal, Enhanced generation of free radicals from phagocytes induced by mineral dusts, Am. J. Respir. Cell. Mol. Biol. 6:404 (1992).
A. J. Ghio, M. B. Kadiiska, Q. H. Xiang and R P. Mason, In vivo evidence of free radical formation after asbestos instillation: an ESR spin trapping investigation, Free Radic. Biol. Med. 24:11 (1998).
T. Ishizaki, E. Yano, N. Urano and P. H. Evans, Crocidolite-induced reactive oxygen metabolites generation from human polymorphonuclear leukocytes, Environ. Res. 66:208 (1994).
T. Takeuchi, K. Morimoto, H. Kosaka and T. Shiga, Spin trapping of superoxide released by opsonized asbestos from human promyelocytic leukemia cell line, HL60, Biochem. Biophys. Res. Commun. 194:57 (1993).
Y. Rojanasakul, X. Shi, D. Deshpande, W. W. Liang and L. Y. Wang, Protection against oxidative injury and permeability alteration in cultured alveolar epithelium by transferrin-catalase conjugate, Biochim. Biophys. Acta. 1315:21 (1996).
W. A. Pryor, Biological effects of cigarette smoke, wood smoke, and the smoke from plastics: the use of electron spinresonance, Free Radic. Biol. Med. 13:659 (1992).
K. K. Stone, E. Bermudez and W. A. Pryor, Aqueous extracts of cigarette tar containing the tar free radical cause DNA nicks in mammalian cells, Environ. Health Perspectives. 102(Suppl 10):173 (1994).
M. Tsuchiya, D. F. Thompson, Y. J. Suzuki, C. E. Cross and L. Packer, Superoxide formed from cigarette smoke impairs polymorphonuclear leukocyte active oxygen generationactivity, Arch. Biochem. Biophys. 299:30 (1992).
K. R. Maples, T. Sandstrom, Y. F. Su and R. F. Henderson, The nitric oxide/heme protein complex as a biologic marker of exposure to nitrogen dioxide in humans, rats, and in vitro models, Am. J. Respir. Cell. Mol. Biol. 4:538 (1991).
I. Ueno, M. Hoshino, T. Miura and N. Shinriki, Ozone exposure generates free radicals in the blood samples in vitro. Detection by the ESR spin-trapping technique, Free Radic. Res. 29: 127 (1998).
B. Gonet, Free radical aspects of the ozone influence on blood, Physiol. Chem. Phys. Med. NMR. 26:273 (1994).
W. A. Pryor, Mechanisms of radical formation from reactions of ozone with target molecules in the lung, Free Radic. Biol. Med. 17:451 (1994).
M. K. Pulatova, V. L. Sharygin and Iu. P. Reva, Detection and nature of melanincontaining centers in bronchoalveolar smears and blood of persons responsible for cleaning up after the accident at the Chernobyl Atomic Energy Station, Dokl. Akad. Nauk. 345: 130 (1995) (Russ.).
S. F. Piao, Studies of free radical metabolism in patients with cor pulmonale, Chung. Hua. Chieh. Ho Ho Hu Hsi Tsa Chih. 15:214, 254 (1992).
G. Supinski, Free radical induced respiratory muscle dysfunction, Mol. Cell. Biochem. 179:99 (1998).
R. F. Baikeev, K. M. Ziiatdinov, I. R. Akhmadeev, G. T. Rakhmaevaand N. G. Demidova, The diagnosis of the destructive changes in pulmonary and osteoarticular tuberculosis, Problemy Tuberkuleza. N11–12:28 (1992) (Russ.).
K. Takeda, M. Haida, S. Shioya, T. Matsumori, Y. Kimura and K. Hasumi, Estimation of the malignancy of pleural effusions by electron spin resonance, Anal. Biochem. 241:47 (1996).
P. E. James, G. Bacic, O. Y. Grinberg, F. Goda, J. F. Dunn, S. K. Jackson and H. M. Swark, Endotoxin-induced changes in intrarenal pO2, measured by in vivo electron paramagnetic resonance oximetry and magnetic resonance imaging, Free Radic. Biol. Med. 21:25 (1996).
K. Gwozdzinski and M. Janicka, Oxygen free radicals and red blood cell damage in acute renal failure, Biochem. Soc. Trans. 23:635S (1995).
J. Pincemail, O. Detry, C. Philippart, J. O. Defraigne, C. Franssen, K. Burhop, C. Deby, M. Meurisse and M. Lamy, Diaspirin crosslinked hemoglobin (DCLHb): absence of increased free radical generation following administration in a rabbit model of renal ischemia and reperfusion, Free Radic. Biol. Med. 19:1 (1995).
Z. Zdrojewski, J. Nowak, A. Raszeja-Specht, A. Skibowska, J. Kustosz and B. Rutkowski, Evaluation of platelet membrane structure in patients with chronic glomerulonephritis (CGN), Przegl. Lek. 53:431 (1996).
D. Roccatello, G. Mengozzi, M. Ferro, G. Cesano, R. Polloni, R. Mosso, G. Bonetti, T. Inconis, L. Paradisi, L. M. Sena and G. Piccoli, Isosorbide 5 mononitrate administration increases nitric oxide blood levels and reduces proteinuria in IGA glomerulonephritis patients with abnormal urinary endothelin cyclic GMP ratio, Clin. Nephrol. 44:163 (1995).
A. Kashem, M. Endoh, F. Yamauchi, N. Yano, Y. Nomoto, H. Sakai, L. Pronai, M. Tanaka and H. Nakazawa, Superoxide dismutase activity in human glomerulonephritis, Am. J. Kidney Dis. 28:14 (1996).
K. Yokoyama, Y. Tomino, Y. Yaguchi, H. Koide, D. Ohmori and F. Yamakura, Serum superoxide dismutase (SOD) activity in patients with renal disease by a spintrap method using electron spin resonance (ESR), Nippon Jinzo Gakkai Shi. 35:809 (1993).
S. E. Roselaar, N. B. Nazhat, P. G. Winyard, P. Jones, J. Cunningham and D. R. Blake, Detection of oxidants in uremic plasma by electron spin resonance spectroscopy, Kidney Int. 48:199 (1995).
H. Trachtman, D. Wilson and P. S. Rao, The role of oxygen free radicals in the development of chronic renal failure, Life Sci. 50: 1877 (1992).
G. M. Bogdan, Blood PMC of Chronic Renal Failure Patients, Thesis Ph.D., Krasnoyarsk (1993) (Russ.).
G. M. Bogdan and R. G. Saifutdinov, Paramagnetic blood centres by patients with chronic renal failure, XXVII-th Congress Ampere, August 21–28, Kazan (1994), pp. 879–880.
V. S. Finin, V. I. Soklakov, N. E. Savchenko and V. A. Deshko, Spin probe study of blood serum on uremia, Ru Fizika i Khimiya Elementarnykh Khimicheskikh Protsessov; V Vserossiiskaya Konferentsiya, Posvyashchennaya 80-letiyu Akademika V.V. Voevodskogo, September 29–October 3, Chernogolovka (1997), pp. 291–293 (Russ.).
W. A. Pettinger, F. G. Soyanco and J. A. Oates, Inhibition of monoamine oxidase in man by furazolidone, Clin. Pharmacol. Ther. 2: 442 (1968).
B. H. Ali, Pharmacology and toxicity of furazolidone in man and animals: some recent research, Gen. Pharmacol. 20:557 (1989).
L. Rossi, I. De Angelis, J. Z. Pedersen, E. Marchese, A. Stammati, G. Rotilio and F. Zucco, N-[5-nitro-2-furfurylidene]-3-amino-2-oxazolidinone activation by the human intestinal cell line Caco-2 monitored through noninvasive electron spin resonance spectroscopy, Mol. Pharmacol. 49:547 (1996).
T. Ozawa and Y. Nakano, The radical scavenging abilities of a new anti-nephritic drug, OPC-15161, Biochem. Mol. Biol. Int. 38:231 (1996).
I. A. Menon, S. D. Persad, H. F. Haberman, P. K. Basu, J. F. Norfray, C. C. Felix and B. Kalyanaraman, Characterization of the pigment from homogentisic acid and urine and tissue from an alkaptonuria patient, Biochem. Cell. Biol. 69:269 (1991).
J. Pincemail, J. O. Defraigne, C. Franssen, P. Bonnet, G. Deby-Dupont, J. Pirenne, C. Deby, M. Lamy, M. Limet and M. Meurisse, Evidence for free radical formation during human kidney transplantation, Free Radic. Biol. Med. 15:343 (1993).
M. J. Payne, A. Chapman and R. Cammack, Evidence for an [Fe]-type hydrogenase in the parasitic protozoan Trichomonas vaginalis, FEBS Lett. 317:101 (1993).
M. S. Vidakovic, G. Fraczkiewicz and J. P. Germanas, Expression and spectroscopic characterization of the hydrogenosomal [2Fe-2S] ferredoxin from the protozoan Trichomonas vaginalis, J. Biol. Chem. 271:14734 (1996).
J. M. Richard, E. E. Creppy, J. L. Benoit-Guyod and G. Dirheimer, Orellanine inhibits protein synthesis in Madin-Darby canine kidney cells, in rat liver mitochondria and in vitro: indication for its activation prior to in vitro inhibition, Toxicology. 67:53 (1991).
J. M. Richard, D. Cantin-Esnault and A. Jeunet, First electron spin resonance evidence for the production of semiquinone and oxygen free radicals from orellanine, a mushroom nephrotoxin, Free Radic. Biol. Med. 19:417 (1995).
H. Oubrahim, J. M. Richard, D. Cantin Esnault, F. Seigle Murandi and F. Trecourt, Novel methods for identification and quantification of the mushroom nephrotoxin orellanine. Thin-layer chromatography and electrophoresis screening of mushrooms with electron spin resonance determination of the toxin, J. Chromatogr. A758:145 (1997).
A. G. Maksina, N. P. Mikaelian, Iu. A. Kniazev and B. A. Dainiak, Structural changes in erythrocyte membranes in diabetes mellitus using spin labelled fatty acids, Biofizika. 37:306 (1992) (Russ.).
C. Watala, Hyperglycaemia alters the physico-chemical properties of proteins in erythrocyte membranes of diabetic patients, Int. J. Biochem. 24:1755 (1992).
E. A. Preoteasa, C. Ionescu-Tirgoviste, V. V. Grecu and R. Georgescu, Electron spin resonance study of the erythrocyte membrane fluidity changes in diabetes, Rom. J. Intern. Med. 31:271 (1993).
S. R. Wente, M. Villalba, V. L. Schramm and O. M. Rosen, Mn2(+)-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor, Proc. Natl. Acad. Sci. USA. 87:2805 (1990).
M. T. Santini, P. L. Indovina, J. R. Simmons and S. W. Peterson, Human erythrocyte insulin receptor down-regulation is accompanied by a transient decrease in membrane order, Biochim. Biophys. Acta. 1054:333 (1990).
M. T. Santini, R Masella, A. Cantafora and S. W. Peterson, Changes in erythrocyte membrane lipid composition affect the transient decrease in membrane order which accompanies insulin receptor down-regulation, Experientia 48:36 (1992).
W. Malorni, R. Masella, M. T. Santini, F. Iosi, P. Samoggia, A. Cantafora, D. Merrell and S. W. Peterson, Human erythrocyte insulin receptor processing is affected by the oxidizing agent menadione, Exp. Cell. Res. 206:195 (1993).
C. J. Mullarkey, D. Edelstein and M. Brownlee, Free radical generation by early glycation products: a mechanism for accelerated atherogenesis in diabetes, Biochem. Biophys. Res. Commun. 173:932 (1990).
M. C. Delmas-Beauview, E. Peuchant, M. J. Thomas, L. Dubourg, A. P. Pinto, M. Clerc and H. Gin, The place of electron spin resonance methods in the detection of oxidative stress in type 2 diabetes with poor glycemic control, Clin. Biochem. 31:221 (1998).
R. G. Saifutdinov and K. A. Apartsin, Spleen tissue paramagnetic centers prior to spleen autotransplantation in experiment and clinics, Aktual’nye Voprosy Rekonstruktivnoii Vosstanovitel’noi Khirurgii, Irkutsk (1993), pp. 197–198 (Russ.).
J. A. Corbett, M. A. Sweetland, J. L. Wang, J. R. Lancaster Jr and M. L. McDaniel, Nitric oxide mediates cytokine-induced inhibition of insulin secretion by human islets of Langerhans, Proc. Natl. Acad.. Sci. USA. 90:1731 (1993).
M. L. Brader, D. Borchardt and M. F. Dunn, The T to R transition in the copper(II)-substituted insulin hexamer. Anion complexes of the R-state species exhibiting type 1 and type 2 spectral characteristics, Biochemistry. 31:4691 (1992).
M. Brank, M. Sentjurc, A. Stalc and Z. Grubic, The influence of soman simulator on reactivation by HI-6 of soman-inhibited acetylcholinesterase in preparations of rat and human skeletal muscle, Biochem. Pharmacol. 45:499 (1993).
D. E. Bredesen, M. Wiedau-Pazos, J. J. Goto, S. Rabizadeh, J. A. Roe, E. B. Gralla, L. M. Ellerby and J. S. Valentine, Cell death mechanisms in ALS, Neurology. 47 (Suppl 2):S36, (discussion S38) (1996).
J. Liu, M. K. Shigenaga, L. J. Yan, A. Mori and B. N. Ames, Antioxidant activity of diethyldithiocarbamate, Free Radic. Res. 24:461 (1996).
E. G. Janzen, Spintrapping, Accounts. Chem. Res. 4:31 (1971).
J. R. Harbour, V. Chow and J. Bolton, An electron spin resonance study of the spin adduct of OH and HO2 radicals with nitrons in the ultra violet photolysis of aqueous hydrogen peroxide solution, Can. J. Chem. 52:3549 (1974).
E. G. Janzen, D. E. Nutter and E. D. Davis, On spin trapping hydroxyl and hydroperoxyl radicals, Can. J. Chem. 56:2237 (1978).
M. Hiramatsu, M. Kohno, R. Edamatsu, K. Mitsuta and A. Mori, Increased superoxide dismutase activity in aged human cerebrospinal fluid and rat brain determined by electron spin resonance spectrometry using the spin trap method, J. Neurochem. 58:1160 (1992).
B. Halliwell and J. M. C. Gutterige, Free Radicals in Biology and Medicine, Clarendon Press, Oxford (1989), pp. 324–332.
R. Nakagawa and N. Tsuchihasi, A free radical in human cerebrospinal fluid investigated by EPR, Chem. Letters. 551 (1997).
T. Tamada, H. Inoue and A. Mori, Superoxide dismutase activity in cerebrospinal fluid and its relation to compression of the lumbosacral nerve root, Acta Med. Okayama 50: 197 (1996).
S. Kaakkola, P. H. Rosenberg, A. Alila, T. Erkinjuntti, R. Sulkava and J. Palo, Platelet membrane fluidity in Alzheimer’s disease and multi-infarct dementia: a spin label study, Acta Neurol. Scand. 84: 18 (1991).
M. Wender, J. Szczech, S. Hoffmann and W. Hilczer, Electron paramagnetic resonance analysis of heavy metals in the aging human brain, Neuropatol. Pol. 30:65 (1992).
K. M. Lundberg, C. J. Stenland, F. E. Cohen, S. B. Prusiner and G. L. Millhauser, Chem. Biol. 4:345 (1997).
D. A. Butterfield, K. Hensley, M. Harris, M. Mattson and J. Carney, β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer’s disease, Biochem. Biophys. Res. Commun. 200:710 (1994).
D. A. Buttefield, K. Hensley, P. Cole, R. Subramanian, M. Aksenov, M. Aksenova, P. M. Bummer, B. E. Haley and J. M. Carney, Oxidatively induced structural alteration of glutamine synthetase assessed by analysis of spin label incorporation kinetics: relevance to Alzheimer’s disease, J. Neurochem. 68:2451 (1997).
D. A. Buttefield, β-Amyloid-Associated free radical oxidative stress and neurotoxicity: implications for Alzheimer’s disease, Chem. Res. Toxicol. 10:495 (1997).
M. E. Harris, J. M. Carney, P. S. Cole, K. Hensley, B. J. Howard, L. Martin, P. Bummer, Y. Wang, N. W. Pedigo Jr and D. A. Butterfield, beta-Amyloid peptide-derived, oxygen-dependent free radicals inhibit glutamate uptake in cultured astrocytes: implications for Alzheimer’s disease, Neuroreport. 6:1875 (1995).
B. Gonthier, H. Eysseric, A. Soubeyran, D. Daveloose, R. Saxod and L. Barret, Free Radic. Res. 27:645 (1997).
Y. Zhou, J. S. Richardson, M. J. Mombourquette and J. A. Weil, Free radical formation in autopsy samples of Alzheimer and control cortex, Neurosci. Lett. 195:89 (1995).
G. Nattero, G. Mengozzi, T. Inconis and L. Paradisi, Nitric oxide, endothelin-1, and transcranial Doppler in migraine. Findings in interictal conditions and during migraine attack, Headache. 36:307 (1996).
S. W. Norby, J. A. Weyhenmeyer and R. B. Clarkson, Stimulation and inhibition of nitric oxide production in macrophages and neural cells as observed by spin trapping, Free Radic. Biol. Med. 22:1 (1997).
L. Zecca, T. Shima, A. Stroppolo, C. Goj, G. A. Battiston, R Gerbasi, T. Sarna and H. M. Swartz, Interaction of neuromelanin and iron in substantia nigra and other areas of human brain, Neuroscience. 73:407 (1996).
S. Aime, B. Bergamasco, D. Biglino, G. Digilio, M. Fasano, E. Giamello and L. Lopiano, Biochim. Biophys. Acta. 1361:49 (1997).
W. S. Enochs, M. J. Nilges and H. M. Swartz, Purified human neuromelanin, synthetic dopamine melanin as a potential model pigment, and the normal human substantia nigra: characterization by electron paramagnetic resonance spectroscopy, J. Neurochem. 61:68 (1993).
L. Mosca, C. Blarzino, R. Coccia, C. Foppoli and M. A. Rosei, Melanins from tetrahydroisoquinolines: spectroscopic characteristics, scavenging activity and redox transfer properties, Free Radic. Biol. Med. 24:161 (1998).
L. Zecca and H. M. Swartz, Total and paramagnetic metals in human substantia nigra and its neuromelanin, J. Neural. Transm. Park. Dis. Dement. Sect. 5:203 (1993).
S. Nishibayashi, M. Asanuma, M. Kohno, M. Gomez-Vargas and N. Ogawa, Scavenging effects of dopamine agonists on nitric oxide radicals, J. Neurochem. 67:2208 (1996).
J. K. Shergill, R. Cammack, C. E. Cooper, J. M. Cooper, V. M. Mann and A. H. Schapira, Detection of nitrosyl complexes in human substantia nigra, in relation to Parkinson’s disease, Biochem. Biophys. Res. Commun. 228:298 (1996).
D. Constantin, A. Bini, E. Meletti, P. Moldeus, D. Monti and A. Tomasi, Age-related differences in the metabolism of sulphite to sulphate and in the identification of sulphur trioxide radical in human polymorphonuclear leukocytes, Mech. Ageing Dev. 88:95 (1996).
M. T. Carri, A. Battistoni, F. Polizio, A. Desideri and G. Rotilio, Impaired copper binding by the H46R mutant of human Cu, Zn superoxide dismutase, involved in amyotrophic lateral sclerosis, FEBS Lett. 356:314 (1994).
D. Rosen, T. Siddique, D. Patterson, D. A. Figlewicz, P. Sapp, A. Hentati, D. Donaldson, J. Goto, J. P. Oregan, H. X. Deng, Z. Rahmani, A. Krizus, D. McKennayasek, A. Cayabyab, S. M. Gaston, R Berger, R. E. Tanzi, J. J. Halperin, W. Y. Hung, T. Bird, G. Deng, D. W. Mulder, C. Smyth, ... J. S. Gusella, H. R. Horvitz and R. H. Brown, Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophiclateral sclerosis, Nature. 362(N6415):59 (1993).
D. E. Bredesen, L. M. Ellerby, P. J. Hart, M. Wiedau-Pazos and J. S. Valentine, Do post tranlational modifications of CuZnSOD lead to sporadic amyotrophic lateral sclerosis?, Annals of Neurology. 42:135 (1997).
G. Ferretti, A. Tangorra and G. Curatola, Effects of intramembrane particle aggregation on erythrocyte membrane fluidity: an electron spin resonance study in normal and in dystrophic subjects, Exp. Cell. Res. 191:14 (1990).
Y. Ihara, A. Mori, T. Hayabara, R. Namba, K. Nobukuni, K. Sato, S. Miyata, R. Edamatsu, J. Liu and M. Kawai, Free radicals, lipid peroxides and antioxidants in blood of patients with myotonic dystrophy, J. Neurol. 242:119 (1995).
M. Rybczynska, A. L. Pawlak, S. K. Hoffmann and R Ignatowicz, Carriers of ataxia-telangiectasiagene display additional protein fraction and changes in the environment of SH groups in erythrocyte membrane, Biochim. Biophys. Acta. 1022:260 (1990).
A. V. Musaev, S. G. Guseinova and A. P. Mamedov, The combined use of electromagnetic decimeter waves and deresinated naphthalan in patients with vertebrogenic humeroscapular periarthrosis (its experimental and clinical validation), Voprosy Kurortol. Fizioter. Lech. Fiz. Kult. 4:9 (1994) (Russ.).
P. J. Bacon, S. A. Love, A. K. Gupta, P. J. Kirkpatrick and D. K. Menon, Plasma antioxidant consumption associated with ischemia reperfusion during carotid endarterectomy, Stroke. 27:1808 (1996).
E. V. Onuchina, Clinical and Diagnostic Value of Paramagnetic Antioxydants in Biological Fluids of Patients with Rheumatoid Arthritis and Osteoarthrosis, Thesis Ph.D., Institute of Rheumatology, Moskva (1993) (Russ.).
E. V. Popova, Yu. A. Goryaev and R. G. Saifutdinov, Differential diagnosis of rheumatoid arthritis and osteoarthrosis deformans, Pat SSSRN 1810829 (1989), Bull Izobr. N15:126 (1993) (Russ.).
E. V. Popova, Yu. A. Goryaev and R. G. Saifutdinov, Differential diagnosis of rheumatoid arthritis activity, Pat SSSRN 1686357 (1989), Bull Izobr. N39:163 (1991) (Russ.).
C. L. Hawkins and M. J. Davies, Direct detection and identification of radicals generated during the hydroxyl radical-induced degradation of hyaluronic acid and related materials, Free Radic. Biol. Med. 21:275 (1996).
A. V. Suchkov and A. I. Sinopal’nikov, Cyanosis, Klinicheskaya Meditsina. 2:63 (1997) (Russ.).
K. Stolze, A. Dadak Y. Liu and H. Nohl, Hydroxylamine and phenol-induced formation of methemoglobin and free radical intermediates in erythrocytes, Biochem. Pharmacol. 52:1821 (1996).
H. Nohl and K. Stolze, The effects of xenobiotics on erythrocytes, Gen. Pharmacol. 31:343 (1998).
R. P. Bonomo, A. De Flora, E. Rizzarelli, A. M. Santoro, G. Tabbi and M. Tonetti, Copper(II) complexes encapsulated in human red blood cells, J. Inorg. Biochem. 59:773 (1995).
D. Singh, N. B. Nazhat, K. Fairbum, T. Sahinoglu, D. R. Blake and P. Jones, Electron spin resonance spectroscopic demonstration of the generation of reactive oxygen species by diseased human synovial tissue following ex vivo hypoxia-reoxygenation, Ann. Rheum. Dis. 54:94 (1995).
L. Pronai, Y. Ichikawa, H. Nakazawa and S. Arimori, Superoxide scavenging activity of leukocytes in rheumatoid arthritis and Behcet’s diseases, Tokai J. Exp. Clin. Med. 15:93 (1990).
G. Saifutdinov and E. V. Onuchina, The activity of glutathione reductase of the red cells of patients with rheumatoid arthritis, XXVII-th Congress Ampere, August 21–28, Kazan (1994), pp. 909–910.
V. P. P. Timofeev, V. A. Lapuk and B. A. Samarianov, Differentiation of the spatial mobility of lysine residues in immunoglobulin G using spin labels, Mol. Biol. (Moskva), 28: 1315 (1994) (Russ.).
R. Chatterjee, U. Bandyopadhyay, A. Mazumdar and R. K. Banerjee, Lactoper-oxidase-catalysed oxidation of indomethacin, a nonsteroidal antiinflammatory drug, through the formation of a free radical, Biochem. Pharmacol. 52:1169 (1996).
S. Sankarapandi and J. L. Zweier, Bicarbonate is required for the peroxidase function of Cu, Zn-superoxide dismutase at physiological pH, J. Biol. Chem. 274:1226 (1999).
C. C. Lin, J. M. Lu, J. J. Yang, S. C. Chuang and T. Ujiie, Anti-inflammatory and radical scavenge effects of Arctium lappa, Am. J. Clin. Med. 24:127 (1996).
R. L. Webber, Oral imaging as a diagnostic tool for assessing osseous changes, J. Bone Miner. Res. Suppl. 2:S543 (1993).
M. C. Symons, Radicals generated by bone cutting and fracture, Free Radic. Biol. Med. 20:831 (1996).
E. S. Green, C. Cooper, J. Wrigglesworth and C. Rice-Evans, A novel hydrogen-donating drug suppresses haem damage from myoglobin mediated by oxidised low density lipoproteins, Biochem. Soc. Trans. 20:330S (1992).
T. Kitagawa, M. R. Ondrias, D. L. Rousseau, M. Ikeda-Saito and T. Yonetani, Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and hemoglobin, Nature. 298(N5877): 869 (1982).
M. Ikeda-Saito, R. S. Lutz, D. A. Shelley, E. J. McKelvey, R. Mattera and H. Hori, Free radicals, lipid peroxides and antioxidants in blood of patients with myotonic dystrophy, J. Biol. Chem. 266:23641 (1991).
K. Yamaguchi, Y. Watanabe and I. Morishima, Push effect on the heterolytic 0-0 bond clevage of peroxoiron (III) porphyrin adducts, Inorg. Chem. 31:156 (1992).
S. Adachi, S. Nagano, K. Ishimori, Y. Watanabe, I. Morishima, T. Egawa, T. Kitagawa and R. Makino, Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase, Biochemistry. 32:241 (1993).
X. Chen, G. Guo and S. Li, A study of human keloid with electron spin resonance, Chung Hua Cheng Hsing Shao Shang Wai KO Tsa Chih. 12:9 (1996).
Z. V. Kuropteva, S. G. Mikaelyan and T. V. Sanikadze, EPR study of skin and liver changes in experimental and clinical bums, Magnitnyi Rezonans v Biologii i Meditsine, Moskva (1981), pp. 221–222 (Russ.).
J. Fuchs, H. J. Freisleben, M. Podda, G. Zimmer, R. Milbradt and L. Packer, Nitroxide radical biostability in skin, Free Radic. Biol. Med. 15:415 (1993).
Y. Kawasaki, D. Quan, K. Sakamoto and H. I. Maibach, Dermatology. 194:238 (1997).
A. Iannone, A. Marconi, G. Zambruno, A. Giannetti, V. Vannini and A. Tomasi, Free radical production during metabolism of organic hydroperoxides by normal human keratinocytes, J. Invest. Dermatol. 101:59 (1993).
K. Mader, G. Bacic and H. M. Swartz, In vivo detection of anthralin-derived free radicals in the skin of hairless mice by low-frequency electron paramagnetic resonance spectroscopy, J. Invest. Dermatol. 104:514 (1995).
H. Zhang and R. L. Zheng, Promotion of human sperm capacitation by superoxide anion, Free Radic. Res. 24:261 (1996).
F. W. Kleinhans, V. S. Travis, J. Du, P. M. Villines, K. E. Colvin and J. K. Critser, Measurement of human sperm intracellular water volume by electron spin resonance, J. Androl. 13:498 (1992).
J. Du, F. W. Kleinhans, P. Mazur and J. K. Critser, Human spermatozoa glycerol permeability and activation energy determined by electron paramagnetic resonance, Biochim. Biophys. Acta. 1194: 1 (1994).
E. N. Burgova, Human and Animal Tissue PMCs in Some Pathological States, Thesis Ph.D., Institute of Chem. Phys. RAS, Moskva (1986) (Russ.).
C. Benedetto, A. Bocci, M. U. Dianzani, B. Ghiringhello, T. F. Slater, A. Tomasi and V. Vannini, Electron Spin Resonance studies on normal human uterus and cervix and on benign and malignant uterine tumors, Cancer Res. 41:2936 (1981).
A. Tomasi, C. Benedetto, M. Nilges, F. Slater, H. M. Swartz and M. C. R. Symons, Studies on human uterine cervix and rat uterus using S-band, X-band and Q-band electron spin resonance spectroscopy, Biochem. J. 224:431 (1984).
D. R. Orazvalieva, S. V. Stepankov, E. N. Burgova, N. I. Zorina and A. F. Vanin, Ribonucleatide reductase paramagnetic form in humantissue, Biofizika. 34:139 (1989) (Russ.).
N. Madan, S. Kapoor, U. Rusia, S. Sharma, V. L. Nayyar, K. R. Sundaram and S. K. Sood ESR and iron status in pregnancy, Indian J. Pathol. Microbiol. 40:521 (1997).
K. Eguchi, T. Sawai, Y. Mizutani and M. Yonezawa, Comparative study of erythrocyte deformability in maternal and cord blood, Am. J. Perinatol. 12:39 (1995).
J Kolena, K Matejcikova and G. Srenkelova, Osmolytes improve the reconstitution of luteinizing hormone/human chorionic gonadotropin receptors into proteoliposomes, Mol. Cell. Endocrinol. 83:201 (1992).
P. Gettins and L. Sottrup-Jensen, NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin, J. Biol. Chem. 265:7268 (1990).
L. Mazzanti, R. A. Rabini, G. Biagini, A. Pugnaloni, R. de Pirro, E. Faloia, V. Mancini, C. Romanini and N. Cester, Changes in membrane fluidity and Na+/K+-ATPase activity during human trophoblast cell culture, Eur. J. Biochem. 206:881 (1992).
A. M. Caccuri, F. Polizio, F. Piemonte, P. Tagliatesta, G. Federici and A. Desideri, Investigation of the active site of human placenta glutathione transferase pi by means of a spin-labelled glutathione analogue, Biochim. Biophys. Acta 1122:265 (1992).
A. Desideri, A. M. Caccuri, F. Polizio, R. Bastoni and G. Federici, Electron paramagnetic resonance identification of a highly reactive thiol group in the proximity of the catalytic site of human placenta glutathione transferase, J. Biol. Chem. 266:2063 (1991).
M. E. Malone, E. A. Martin, R. M. Jones, R Jukes, C. K. Lim, L. L. Smith and I. N. White, Peroxidase activation of 4-hydroxytamoxifen to free radicals detected by EPR spectroscopy, Free Radic. Biol. Med. 22:423 (1997).
M. A. Foster, ESR in haematological research, Br. J. Haematol. 47:1 (1981).
C. Mailer, H. M. Swartz, M. Konieczny, et al., Identify of the paramagnetic element found in increased concentrations inplasma of cancer patients and its relationship to other pathological processes, Cancer Res. 34:637 (1974).
E. P. Sidorik, L. M. Korchevaya and A. P. Burlaka, Bile EPR study in tumor process diagnosis, Onkologiya (Kiev). 14:68 (1979) (Russ.).
X. Li, Active oxygen radicals produced by the leukocytes in patients with malignant lymphoma, Chung Hua I Hsueh Tsa Chih. (Taipei). 70:334, 24 (1990).
C. E. Cooper, G. R. Lynagh, K. P. Hoyes, R. C. Hider, R. Cammack and J. B. Porter, The relationship of intracellular iron chelation to the inhibition and regeneration of human ribonucleotide reductase, J. Biol. Chem. 271:20291 (1996).
N. Miyoshi, V. MisHk and P. Riesz, Sonodynamic toxicity of gallium-porphyrin analogue ATX-70 in human leukemia cells, Radiat. Res. 148:43 (1997).
K. Satoh and H. Sakagami, Effect of copper and iron ions on cytotoxicity induced by ascorbate, gallate and caffeate, Anticancer Res. 17:2181 (1997).
A. Nogaki, K. Satoh, K. Iwasaka, H. Takano, M. Takahama, Y. Ida and H. Sakagami, Radical intensity and cytotoxic activity of curcumin and gallic acid, Anticancer Res. 18:3487 (1998).
K. J. Res P. Bilski, C. F. Chignell, J. A. Hartley, N. Khan, R. L. Souhami, A. J. Mendonca and J. W. Lown, Photosensitization by anticancer agents. 11. Mechanisms of photosensitization of human leukemic cells by diaminoanthraquinones: singlet oxygen and radical reactions, J. Photochem. Photobiol. B15:317 (1992).
G. Lassmanm, B. Liermann, W. Arnold and K. Schwabe, Ribonucleotide reductase in melanoma tissue. EPR detection in human amelanotic melanoma and quenching of the tyrosine radical by 4-hydroxyanisole, J. Cancer Res. Clin. Oncol. 117:91 (1991).
K. U. Schallreuter, T. E. Elgren, L. S. Nelson Jr, S. MacFarlan, I. Yan-Sze and H. P. Hogenkamp, Ribonucleotide diphosphate reductase from human metastatic melanoma, Melanoma Res. 2:393 (1992).
S. L. Baader, E. Bill, A. X. Trautwein, G. Bruchelt and T. Matxanke, Mobilization of iron from cellular ferritin by ascorbic acid in neuroblastoma SK-N-SH cells: an EPR study, FEBS Lett. 381:131 (1996).
M. Yang, N. B. Nazhat, X. Jiang, S. M. Kelsey, D. R Blake, A. C. Newland and C. J. Moms, Adriamycin stimulates proliferation of human lymphoblastic leukaemic cells via a mechanism of hydrogen peroxide (H2O2) production, Br. J. Haematol. 95:339 (1996).
B. L. Samuels, J. L. Murray, M. B. Cohen, A. R. Safa, B. K. Sinha, A. J. Townsend, M. A. Beckett and R. R Weichselbaum, Increased glutathione peroxidase activity in a human sarcoma cell line with inherent doxorubicin resistance, Cancer Res. 51:521 (1991).
E. G. Mimnaugh, C. R. Fairchild, J. P. Fruehauf and B. K. Sinha, Biochemical and pharmacological characterization of MCF-7 drug-sensitive and AdrR multidrug-resistant human breast tumor xenografts in athymic nude mice, Biochem. Pharmacol. 42:391 (1991).
E. E. Voest, E. Van Faassen, J. P. Neijt, J. J. Marx and B. S. Van Asbeck, Doxorubicin-mediated flee radical generation in intact human tumor cells enhances nitroxide electron paramagnetic resonance absorption intensity decay, Magn. Reson. Med. 30:283 (1993).
L. Dusre, S. Rajagopalan, H. M. Eliot, J. M. Covey and B. K. Sinha, DNA interstrand cross-link and free radical formation in a human multidrug-resistant cell line from mitomycin C and its analogues, Cancer Res. 50:648 (1990).
A. J. Townsend, C. S. Morrow, B. K. Sinha and K. H. Cowan, Selenium-dependent glutathione peroxidase expression is inversely related to estrogen receptor content of human breast cancer cells, Cancer Commun. 3:265 (1991).
A. Ask, L. Persson, A. Rehnholm, L. Frostesjo, I. Holm and O. Heby, Development of resistance to hydroxyurea during treatment of human myelogenous leukemia K562 cells with alpha-difluoromethylornithine as a result of coamplification of genes for ornithine decarboxylase and ribonucleotide reductase R2 subunit, Cancer Res. 53:5262 (1993).
J. Z. Pedersen, L. Marcocci, L. Rossi, I. Mavelli and G. Rotilio, Generation of daunomycin radicals on the outer side of the erythrocyte membrane, Biochem. Biophys. Res. Commun. 168:240 (1990).
H. Sakagami, K. Satoh, K. Sugaya, M. Iida, N. Hirota, K. Matsumoto, S. Kimura, K. Gomi, S. Taguchi, S. Kato and M. Takeda, Effect of the type of serum in the medium on sodium ascorbate-induced cytotoxicity, Anticancer Res. 16:1937 (1996).
S. L. Schrier, A. Zachowski and P. F. Devaux, Mechanisms of amphipath-induced stomatocytosis in human erythrocytes, Blood. 79:782 (1992).
L. M. Nutter, Y. Y. Wu, E. O. Ngo, E. E. Sierra, P. L. Gutierrez and Y. J. Abul-Haj, An o-quinone form of estrogen produces free radicals in human breast cancer cells: correlation with DNA damage, Chem. Res. Toxicol. 7:23 (1994).
E. E. Voest, E. van Faassen, B. S. van Asbeck, J. P. Neijt and J. J. Marx, Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical, Biochim. Biophys. Acta. 1136: 113 (1992).
S. Mishra, A spin decay assay for tumor necrosis factor cytotoxicity, Indian J. Biochem. Biophys. 32:254 (1995).
D. Nichiporov, V. Kostjuchenko, J. M. Puhl, D. L. Bensen, M. F. Desrosiers, C. E. Dick, W. L. McLaughlin, T. Kojima, B. M. Coursey and S. Zink, Investigation of applicability of alanine and radiochromic detectorsto dosimetry of proton clinical beams, Appl. Radiat. Isot. 46:1355 (1995).
B. Stone, J. M. Brown, T. L. Phillips and R. M. Sutherland, Oxygen in human tumors: correlations between methods of measurement and response to therapy, Summary of a Workshop, Bethesda, Maryland, November 19–20 (1992), Radiat. Res. 136:422 (1993).
M. Swartz, K. J. Liu, F. Goda and T. Walczak, India ink: a potential clinically applicable EPR oximetry probe, Magn. Reson. Med. 31:229 (1994).
H. M. Swartz, G. Bacic, B. Friedman, F. Goda, O. Grinberg, P. J. Hoopes, J. Jiang, K. J. Liu, T. Nakashima, O’Hara J, et al., Measurements of pO2 in vivo, including human subjects, by electron paramagnetic resonance, Adv. Exp. Med. Biol. 361:119 (1994).
J. A. O’Hara, F. Goda, K. J. Liu, G. Bacic, P. J. Hoopes and H. M. Swartz, The pO2 in a murine tumor after irradiation: an in vivo electron paramagnetic resonance oximetry study, Radiat. Res. 144:222 (1995).
C. Giulivi and E. Cadenas, Extracellular activation of fluorinated aziridinylbenzo-quinone in HT 29 cells EPR studies, Chem. Biol. Interact. 113:191 (1998).
X. B. Qiu and E. Cadenas, The role of NAD(P)H:quinone oxidoreductase in quinone-mediated p21 induction in human colon carcinoma cells, Arch. Biochem. Biophys. 346:241 (1997).
H. Fujiwara, N. Tanaka and T. Suzuki, The effects of anti-cataract drugs on free radicals formation in lenses, Nippon Ganka Gakkai Zasshi. 95:1071 (1991).
H. Fujiwara, Y. Takigawa, T. Suzuki and K. Nakata, Superoxide dismutase activity in cataractous lenses, Jpn. J. Ophthalmol. 36:273 (1992).
M. A. Babizhayev, B. A. Dainyak and A. H. Maxina, ESR spin label and ultrastructural monitoring of protein-lipid interactions in the lens fiber-cell plasma membranes in relation to human ageing and cataractogenesis, Mech. Ageing Dev. 64: 133 (1992).
Y. Obara, The oxidative stress in the cataract formation, Nippon Ganka Gakkai Zasshi. 99:1303 (1995).
N. H. Ansari, L. Wang, A. A. Erwin and D. F. Church, Glucose-dependent formation of free radical species in lens homogenate, Biochem. Mol. Med. 59:68 (1996).
A. B. Guliaev, A. E. Dontsov, V. B. Il’iasova and M. A. Ostrovskii, Determination of the melanin level in human melanosomes in the pigment epithelium of the eye depending on age, Dokl. Akad. Nauk. 333:257 (1993) (Russ.).
M. Rybanowska, A. Bober, J. M. Burke and T. Sama The role of retinal pigment epithelium melanin in photoinduced oxidation of ascorbate, Photochem. Photobiol. 65:472 (1997).
K. Reszka, G. E. Eldred, R. H. Wang, C. Chignell and J. Dillon, The photochemistry of human retinal lipofuscin as studied by EPR, Photochem. Photobiol. 62:1005 (1995).
D. A. Stoyanovsky, R. Goldman, R. M. Darrow, D. T. Organisciak and V. E. Kagan, Endogenous ascorbate regenerates vitamin E in the retina directly and in combination with exogenous dihydrolipoic acid, Curr. Eye Res. 14: 181 (1995).
A. Mazumdar, S. Adak R. Chatterjee and R. K. Banerjee, Mechanism-based inactivation of lacrimal-gland peroxidase by phenylhydrazine: a suicidal substrate to probe the active site, Biochem. J. 324:713 (1997).
A. I. Mikhailov, I. A. Shilova, M. G. Keshelava and A. A. Kivaev, An application of spin-labeling medicine analogs for investigation of the diffusion processes in mild contact lenses, Fizika i Khimiya Elementarnykh Khimicheskikh Protsessov, Ru V Vserossiiskaya Konferentsiya, Posvyashchennaya 80-letiyu Akademika V.V. Voevodskogo, September 29–October 3, Chernogolovka (1997), pp. 298–299 (Russ.).
V. D. Dragomiretskii, Yu. I. Bazhora and A. G. Zazhivilov, A comprehensive study of URT mucous membrane immunity, Ru VII S’ezd Otorinolaringologov Ukrainskoi SSR, Kiev (1989), p. 302 (Russ.).
H. H. Naumann, The mechanism of the respiratory mucosa to wards infections, Acta otolaryng. 89: 165 (1980).
L. G. Tsirul’nikov, V. Ya Kunel’skaya and B. V. Starosvetskii, Lipid peroxidation in patients with chronic pharyngitisis of fungal etiology, Zhurnal Ushnykh, Nosovykh i Gorlovykh Boleznei. N6:45 (1990) (Russ.).
0. A. Azizova, A. I. Islomov and D. I. Roshchupkin, Free radicals of lipid biological membranes after exposure to UV-irradiation, Biofizika. 24:396 (1979) (Russ.).
A. G. Shanturov, R. G. Saifutdinov and E. V. Nosulya, EPR Spectroscopy in Clinical Rhinology, Vostochno-Sibirskoe Knizhnoe Izdatelstvo, Irkutsk (1992) (Russ.).
E. V. Nosulya and R G. Saifutdinov, Diagnostic importance of nasal secretion free radical EPR study, Fizika i Khimiya Elementarnykh Khimicheskikh Protsessov, Ru V Vserossiiskaya Konferentsiya, Posvyashchennaya 80-letiyu Akademika V.V. Voevodskogo, September 29–October 03, Chemogolovka (1997), pp. 275–276 (Russ.).
A. G. Shanturov, E. V. Nosulia and R. G. Saifutdinov, Free Radicals of nasal secretion: the nature and diagnostic importance in chronic non-specific diseases of upper respiratory tract, 27th Congress Ampere, August 21–28, Kazan (1994), pp. 912–913.
S. Z. Piskunov, The Functional Diagnosis and Treatment of Different Rhinitis Forms, Thesis Dr.Sci., Nauchno-Issledovatel’skii Institut Ukha, Gorla, Nosa i Rechi., Moskva, (1986) (Russ.).
G. V. Lavrenova, Nasal Cavity Mucociliar System on Chronic Dust Action, Thesis Dr.Sci., Nauchno-Issledovatel’skii Institut Ukha, Gorla, Nosa i Rechi, Leningrad, (1986) (Russ.).
E. V. Nosulya, A. G. Shanturov and R. G. Saifutdinov, Diagnosis of maxillary sius cysts, Pat SSSRN 1826165, (1991) (Russ.).
D. Passali and L. Bellussi, Circadian changes in the secretory sctivity of nasal mucosa, Acta otolaryngol. 106:281 (1998).
A. V. Kozlov, D. Yu. Egorov, Yu. A. Vladimirov and S. A. Azizova, The formation of iron-ascorbic acid complexes in tissues, Biofizika. 35513 (1990) (Russ.).
E. G. Nosulya, High Respiratory Chronic Disease: Diagnostic and Pathogenetic Role of Nasal Secret PMC, Thesis Dr.Sci., Nauchno-Issledovatel’skii Institut Ucha, Gorla, Nosa i Rechi, Sankt-Peterburg (1994) (Russ.).
A. Yu. Krotov, Vital problems of otorhinolaryngology, Aktual’nye Voprosy Otorinolaringologii, Alma-Ata (1989), pp. 109–111 (Russ.).
B. Majumbar and P. D. Bull, The incidence and bacterilogy of maxillary sinusitis in nasal polyposis, J. Laryng. 96:937 (1982).
J. V. Bannister, W. H. Bannister, H. A. 0. Hill and P. J. Thornally, Enhanced production of hydroxyl radicals by the xanthine-xanthine oxidase reaction in the presence of lactoferrin, Biochim. Acta 715: 116 (1982).
A. G. Shanturov, E. V. Nosulya, R. G. Saifutdinov and E. A. Shpakova, Faucial tonsilla tissues PMCs in patientes with chronic tonsilitis, in: Aktual’nye Voprosy Klinicheskoi Meditsiny, Medical Universuty, Irkutsk (1997), pp. 366–367 (Russ.).
M. F. Ottaviani, A. Fiorini, P. N. Mason and C. Corvaja, Electron spin resonance studies of dental composites: effects of irradiation time, decay over time, pulverization, and temperature variations, Dent. Mater. 8:118 (1992).
H. G. Goetzke and J. Klammt, Size of wound area and frequency of alveolitis after tooth extraction, Dtsch. Z. Mund. Kiefer. Gesichtschir. 15:306 (1991).
H. G. Goetzke and B. Ebert, Experimental studies of the size of the root surface of permanent human teeth, Anat. Anz. 172:117 (1991).
A. Hochi, M. Furusawa and M. Ikeya, Applications of microwave scanning ESR microscope: human tooth with metal, Appl. Radiat. Isot. 44:401 (1993).
S. Mascarenhas, A. Hasegawa and K. Takeshita, ESR dosimetry of bones from Hiroshima A-bomb site, Bull. Amer. Phys. Soc. 18:579 (1973).
B. Pass and J. E. Aldrich, Dental enamel as in vivo dosimetr, Med. Phys. 12:305 (1985).
J. E. Aldrich and B. Pass, Dental Enamel as an in vivo radiation dosemeter: separation of the diagnostic X ray dose from the dose due to natural sources, Radiation. Protection Dosimetry. 17:175 (1986).
I. Caracelli, M. C. Terrile and S. Mascarenhas, ESR and dosimetric properties of bones, Health Phys. 50:259 (1986).
Y Nishiwaki and T. Shimano, Uncertainties in dose estimation under emergency conditions and ESR dosimetry with human teeth, Radiat. Protect. Dosim. 34:295 (1990).
B. Pass, J. E. Aldrich and P. L. Scallion, An analysis of paramagnetic centers in irradiated dentin using electron spin resonance, Calcif. Tissue. Int. 46:166 (1990).
E. J. Rhodes and R. Grun, ESR behavior of the paramagnetic centre at g=2.0018 in tooth enamel, Third International Symposium on ESR Dosimetry and Applications, October 14–18, Japan (1991), p. 62.
E. J. Rhodes and R. Grun, ESR behavior of the paramagnetic centre at g=2.0018 in tooth enamel, Ancient. 9:14 (1991).
M. F. Desrosiers, M. J. Avila, D. A. Schauer, B. M. Coursey and N. J. Parks, Experimental validation of radiopharmaceutical absorbed dose to mineralized bone tissue, Appl. Radiat. Isot. 44:459 (1993).
T. Straume, L. R. Anspaugh, E. H. Haskell, J. N. Lucas, A. A. Marchetti, I. A. Likhtarev, V. V. Chumak A. A. Romanyukha, V. T. Khrouch, Y. I. Gavrilin and V. F. Minenko, Emerging technological bases for retrospective dosimetry. Radiation injury and the chemobyl catastrophe, Stem. Cells (Alpha Med Press), 15 (Supl l2): 183 (1997).
A. I. Ivannikov, V. G. Skvortzov, V. F. Stepanenko, D. D. Tikunov, I. M. Fedosov, A. A. Romanyukha and A. Wieser, Wide-scale EPR retrospective dosimetry: results and problems, Radiat. Protect. Dosimetry. 71:175 (1997).
E. H. Haskell, R. B. Hayes and G. H. Kenner, An EPR dosimetry method for rapid scanning of children following a radiation accident using deciduous teeth, Health Phys. 76: 137 (1999).
B. Pass, A. E. Baranov, E. D. Kleshchenko, J. E. Aldrich, P. L. Scallion and R. P. Gale, Collective biodosimetry as a dosimetric “gold standard”: a study of three radiation accidents, Health Phys. 72:390 (1997).
A. A. Romanyukha, D. Regulla, E. Vasilenko and A. Wieser, South Ural nuclear workers: comparison of individual doses from retrospective EPR dosimetry and operational personal monitoring, Appl. Radiat. Isot. 45: 1195 (1994).
A. Wieser, E. Haskell, G. Kenner and F. Bruenger, EPR dosimetry of bone gains accuracy by isolation of calcified tissue, Appl. Radiat. Isot. 45:525 (1994).
F. Callens, P. Moens and R. Verbeeck, An EPR study of intact and powdered human tooth enamel dried at 400 degrees C, Calcif. Tissue Int. 56:543 (1995).
F. Callens, M. Verbeeck, P. Matthys, L. Martens and E. Boesman, The contribution of CO3(3−) and CO2(−) to the ESR spectrum near g=2 of powdered human tooth enamel, Calcif. Tiss Int. 41:124 (1987).
A. Rossi and G. Poupeau, Radiation damage in bioapatites: the ESR spectrum of irradiated dental enamel revisited, Nucl. Tracks. Radiat. Meas. 17:537 (1990).
M. Ikeya, J. Mijajima and S. Okajima, ESR dosimetry for atomic bomb survivors using shell buttons and tooth enamel, Jap. J. Appl. Phys. 23:L697 (1984).
M. Ikeya, New Applications of ESR. Dating, Dosimetry and Microscopy, World Scientific, Singapore (1993).
H. Schwarcz, ESR studies of tooth enamel, Nucl. Tracks. 10:865 (1985).
N. Nakamura, C. Miyazawa, M. Akiyama, S. Sawada and A. A. Awa, Biodosimetry: chromosome aberration in lymphocytes and electron paramagnetic resonance in tooth enamel from atomic bomb survivors, World Health Stat. Q. 49:67 (1996).
G. Liidja, J. Past, J. Puskar and E. Lippmaa, Paramagnetic resonance in tooth enamel created by ultraviolet light, Appl. Radiat. Isot. 47:785 (1996).
M. Iwasaki, C. Miyazawa and T. Shimano, Relation between the weight of human tooth enamel and the CO3(3−) signal intensity on the ESR dosimetry, Ohu Daigaku Shigakushi. 17:95 (1990).
M. Iwasaki, C. Miyazawa and T. Shimano, A problem with ESR dosimetry utilizing human tooth enamel in low dose region, Ohu Daigaku Shigakushi. 17:303 (1990).
E. A. Ignatiev, A. A. Romanyukha, A. A. Koshta and A. Wieser, Selective saturation method for EPR dosimetry with tooth enamel, Appl. Radiat. Isot. 47:333 (1996).
E. A. Ignatiev, EPR Spectroscopy as a Dosimetry Method in Carbonated Hydroxy Apatite, Thesis Ph.D., Ural University, Ekaterinburg (1998) (Russ.).
V. Skvortzov, A. Ivannikov and U. Eichhoff, Assessment of individual accumulated irradiation dose using EPR spectroscopy of tooth enamel, J. Molec. Struct. 347:321 (1995).
J. E. Aldrich, B. Pass and C. Mailer, Changes in the paramagnetic centres in irradiated and heated dental enamel studied using EPR, Int. J. Radiat. Biol. 61:433 (1992).
T. Room, G. Liidja and E. Lippmaa, Temperature and frequency effects in tooth enamel electron spin resonance dosimetry, Appl. Radiat. Isot. 45: 1061 (1994).
V. E. Galtsev, E. V. Galtseva, O. Ia. Grinberg and Ia. S. Lebedev, Increase in sensitivity of ESR-dosimetry from tooth enamel, Dokl. Akad. Nauk. 334:649 (1994) (Russ.).
J. Aldrich and B. Passm, Determining radiation exposure from nuclear accidents and atomic tests using dental enamel, Health Physics. 54:469 (1988).
G. A. Klevezal, V. A. Serezhenkov and V. N. Kalyakin, Radiation dosage accumulated by reindeer from Novaya Zemlya, Appl. Radiat. Isot. 46: 1077 (1995).
J. Tatsumi-Miyajima and S. Okajima, Physical dosimetry at Nagasaki-Europium-152 of stone embankment and electron spin resonance of teeth from atomic bomb survivors, J. Radiat. Res. (Tokyo). (Suppl 32):83 (1991).
N. Nakamura, C. Miyazawa, S. Sawada, M. Akiyama and A. A. Awa, A close correlation between electron spin resonance (ESR) dosimetry from tooth enamel and cytogenetic dosimetry from lymphocytes of Hiroshima atomic-bomb survivors, Int. J. Radiat. Biol. 73:619 (1998).
N. Nakamura, J. F. Katanic and C. J. Miyazawa, Contamination from possible solar light exposures in ESR dosimetry using human tooth enamel, Radiat. Res. (Tokyo). 39:185 (1998).
A. A. Romanyukha, M. O. Degteva, V. P. Kozheurov, A. Wieser, P. Jacob, E. A. Ignatiev and M. I. Vorobiova, Pilot study of the Urals population by tooth EPR dosimetry, Radiat. Environ. Biophys. 35:305 (1996).
A. A. Romanyukha and D. Regulla, Aspects of retrospective ESR dosimetry (Invited Paper), Appl. Radiat. Isot. 47:293 (1996).
A. A. Romanyukha, D. Regulla, E. Vasilenko, A. Wieser, E. G. Drozhko, A. F. Lyzlov, N. A. Koshurnikova, N. S. Shilnikova and A. P. Panfilov, Verification of occupational doses at the first nuclear plant in the Former Soviet Union, Appl. Radiat. Isot. 47:1277 (1996).
A. A. Romanyukha, E. A. Ignatiev, M. O. Degteva, V. P. Kozheurov, A. Wieser and P. Jacob, Radiation doses from Ural region [letter], Nature. 381(N6579):199 (1996).
A. A. Romanyukha, A. Wieser and D. Regulla, EPR dosimetry with different biological and synthetic carbonated materials, Radiation Protect. Dosimetry. 65:389 (1996).
A. A. Wieser, A. A. Romanyukha, M. O. Degteva, V. P. Kozheurov and G. Petzoldt, Tooth enamel as a natural veta dosimeter for bone seeking radionuclides, Radiat. Protect. Dosimetry. 65:413 (1996).
M. Bauchinger, K. Salassidis, H. Braselmann, A. Vozilova, S. Pressl, G. Stephan, G. Snigiryova, V. P. Kozheurov and A. Akleyev, FISH-based analysis of stable translocations in a Techa River population, Int. J Radiat. Biol. 73:605 (1998).
O. V. Aleinikov, V. S. Finin, V. A. Deshko and A. V. Alekseichik, EPR dosimetry measuring of radioactive irradiation doses in oncohematological children, Fizika i Khimiya Elementarnykh Khimicheskikh Protsessov, Ru V Vserossiiskaya Konferentsiya, Posvyashchennaya 80-letiyu Akademika V.V. Voevodskogo, September 29–October 3, Chernogolovka (1997), pp. 190–191 (Russ.).
E. H. Haskell, G. H. Kenner and R. B. Hayes, Electron paramagnetic resonance dosimetry of dentine following removal of organic material, Health Phys. 68:579 (1995).
T. Shimano, M. Iwasaki, C. Miyazawa, T. Miki, A. Kai and M. Ikeya, Human tooth dosimetry for gamma-rays and dental X-rays using ESR, Appl. Radiat Isot. 40:1035 (1989).
M. Desrosiers, M. Simic, F. Eichmiller, F. Johnston and R. Bowen, Mechanically induced generation of radicals in tooth enamel, Appl. Radiat. Isot. 40: 1195 (1989).
M. F. Desrosiers and A. A. Romanyukha, Technical aspects of the EPR method for tooth enamel dosimetry, in: Biomarkers: Medical and Workplace Application, M. L. Mendelson, L. C. Mohr and J. P. Peters, eds., DC: Josef Henry Press, Washington (1998).
V. Polyakov, E. Haskell, G. Kenner, G. Huett and R. Hayes, Effect of mechanically induced background signal on EPR dosimetry of tooth enamel, Radiat. Meas. 24:249 (1995).
C. Yamanaka, M. Ikeya and H. Hara, In vivo ESR dosimeter for human tooth enamel, Third International Symposium on ESR Dosimetry and Applications, October 14–18, Japan (1991), p.23.
C. Yamanaka, M. Ikeya and H. Hara, ESR cavities for in vivo dosimetry of tooth enamel, Appl. Radiat. Isot. 44:77 (1993).
S. L. Breen and J. J. Battista, Radiation dosimetry in human bone using electron paramagnetic resonance, Phys. Med. Biol. 40:2065 (1995).
M. F. Desrosiers, EPR dosimetry following the San Salvador radiation accident, Third International Symposium on ESR Dosimetry and Applications, October 14–18, Japan (1991), p. 24.
L. A. Blumenfel’d and A. E. Kalmanson, EPR spectra of biological samples, Biofizika 2:552 (1957) (Russ.).
S. Onori, F. dErrico, C. De Angelis, E. Egger, P. Fattibene and I. Janovsky, Alanine dosimetry of proton therapy beams, Med. Phys. 24:447 (1997).
R. Kudynski, J. Kudynska and H. A. Buckmaster, The decay constant for irradiated human hair using EPR spectroscopy, Appl. Radiat. Isot. 45:545 (1994).
V. G. Bebeshko, V. I. Klimenko, L. N. Iukhimuk and I. M. Pogontseva, The paramagnetic centers of the blood in persons with a history of acute radiation sickness as a result of the accident at the Chernobyl Atomic Electric Power Station, Lik. Sprava 4:7 (1992).
W. Kreisel, International program on the health effects of the Chernobyl accident, Stem. Cells (Dayt). Suppl 1:33 (1995).
N. J. Dodd, Free radicals and food irradiation, Biochem. Soc. Symp. 61:247 (1995).
H. Delincee, International cooperation on the detection of irradiated food, Z. Lebensm. Unters. Forsch. 197:217 (1993).
J. Mischke, N. Helle, B. Linke, G. A. Schreiber and K. W. Bogl, Electron spin resonance measurements on dried fruit, Carbohydrate composition and ESR signal structure of irradiated fruit, Z. Ernahrungswiss. 33:258 (1994).
N. Helle, A. Wolbert, B. Linke, D. Ehlers and K. E. Kruger, Electron spin resonance spectroscopy investigations of fresh fruit. Evidence of treatment with ionizing radiation, Z. Lebensm. Unters. Forsch. 201:355 (1995).
T. Miyazaki, T. Kaneko, T. Yoshimura, A. S. Crucq and B. Tilquin, Electron spin resonance study of radiosterilization of antibiotics: ceftazidime, J. Pharm. Sci. 83:68 (1994).
T. Miyazaki, J. Arai, T. Kaneko, K. Yamamoto, M. Gibella and B. Tilquin, Electron spin resonance study of radiosterilization of antibiotics: ceftazidime, J. Pharm. Sci. 83: 1643 (1994).
V. E. Kholmogorov, Photoinduced paramagnetic centers in human blood, Biofizika. 39:888 (1994) (Russ.).
M. Koter, Effect of hyperthermia on the internal microviscosity of erythrocytes and lymphocytes: a spin-label study, Int. J. Radiat. Biol. 58:157 (1990).
O. Korkmaz and M. Korkmaz, The effects of mitomycin-C and temperature on dynamical properties of human erythrocyte membrane, Biophys. Chem. 69:167 (1997).
W. Malorni, S. Paradisi, F. Iosi and M. T. Santini, Two different pathways for necrotic cell death induced by free radicals, Cell. Biol. Toxicol. 9:119 (1993).
J. J. Eckburg, J. C. Chato, K. J. Liu, M. W. Grinstaff, H. M. Swartz, K. S. Suslick and F. P. Auteri, The measurement of temperature with electron paramagnetic resonance spectroscopy, J. Biomech. Eng. 118:193 (1996).
P. J. Halsall, F. R. Ellis and P. F. Knowles, Evaluation of spin resonance spectroscopy of red blood cell membranes to detect malignant hyperthermia susceptibility [see comments], Br. J. Anaesth. 69:471 (1992).
S. K. Sedov, The Influence of the Sanitary-hygienic Condition of Labour on the Healthy of the Foundry Workers, Thesis Ph.D., Institute Prof patologii, Moskva (1983) (Russ.).
A. F. Vanin, L. V. Vakhnina and A. G. Chetverikov, On nature EPR signal in cancer tissues, Biofizika. 15:1044 (1970) (Russ.).
C. K. Narkowicz, J. H. Vial and P. W. McCartney, Hyperbaric oxygen therapy increases free radical levels in the blood of humans, Free Radic. Res. Commun. 19:71 (1993).
M. Minetti, T. Forte, M. Soriani, V. Quaresima, A. Menditto and M. Ferrari, Iron-induced ascorbate oxidation in plasma as monitored by ascorbate free radical formation. No spin-trapping evidence for the hydroxyl radical in iron-overloaded plasma, Biochem. J. 282 (Pt 2):459 (1992).
A. Burt, I. B. Abramov and V. I. Sachkov, Is fluidization of the phospholipid bilayer by general anesthetics a reason for general anesthesia? Bull. Eksp. Biol. Med. 112:387 (1991) (Russ.).
L. Mazzanti, R. A. Rabini, R Staffolani, G. Benedetti, N. Cester and G. Lenaz, Modifications induced by general anesthetics on Na+/K+ ATPase obtained from human placenta, Biochem. Biophys. Res. Commun. 173:1248 (1990).
M. Kudou, T. Kudou and A. Matsuki, Changes in plasma superoxide dismutase like activity during general anesthesia and surgery in man, Masui. 39:1172 (1990).
S. Shirasaki, M. Kudo, H. Ishihara, A. Matsuki and T. Takazawa, The effect of enflurane anesthesia on plasma superoxide dismutase (SOD)-like activity in elderly patients, Masui. 40: 1079 (1991).
K. Gwozdzinski, A spin label study of the action of cupric and mercuric ions on human red blood cells, Toxicology. 65:315 (1991).
R. P. Mason, In vitro and in vivo detection of free radical metabolites, with electron spin resonance, in: Free Radicals. A Practical Approach, N. A, Punchard, F. J. Kelly, eds., Oxford University Press, New York (1996), pp. 12–24.
R. P. Mason, Electron spin resonance investigation of free radical toxicology, in: Free Radicals in Biology and Environment, F. Minisci., ed., Kluwer Academic Publishers, The Netherlands (1997), pp. 1–27.
K. Minakata, O. Suzuki, S. Saito and N. Harada, Ascorbate radical levels in human sera and rat plasma intoxicated with paraquat and diquat, Arch. Toxicol. 67:126 (1993).
J. Lee, C. H. Trad and D. A. Butterfield, Electron paramagnetic resonance studies of the effects of methoxyacetic acid, a teratologic toxin, on human erythrocyte membranes, Toxicology. 83:131 (1993).
A. Constantinescu, H. Tritschler and L. Packer, a-Lipoic acid protects against hemolysis of human erythrocytes induced by peroxyl radicals, Biochem. Mol. Biol. Int. 33:669 (1994).
S. D. Aust, C. F. Chignell, T. M. Bray, B. Kalyanaraman and R. P. Mason, Free radicals in toxicology, Toxicol. Appl. Pharmacol. 120:168 (1993).
G. F. Weber, The measurement of oxygen-derived free radicals and related substances in medicine, J. Clin. Chem. Clin. Biochem. 28:569 (1990).
W. A. Pryor and S. S. Godber, Noninvasive measures of oxidative stress status in humans, Free Radic. Biol. Med. 10:177 (1991).
Yu. V. Zobnin, R. G. Saifutdinov and I. P. Provado, The influence of hemosorption on the contens of the paramagnetic centres in the patients with opium abstinence, XXVII-th Congress Ampere, August 21–28, Kazan (1994), pp. 927–928.
H. F. Galley, M. J. Davies and N. R. Webster, Xanthine oxidase activity and free radical generation in patients with sepsis syndrome, Crit. Care Med. 24:1649 (1996).
A. Fraticelli, C. V. Serano Jr, B. S. Bochner, M. C. Capogrossi and J. L. Zweier, Hydrogen peroxide and superoxide modulate leukocyte adhesion molecule expression and leukocyte endothelial adhesion, Biochim. Biophys. Acta. 1310:251 (1996).
L. A. Sadokhina, A Study of NO Endogenous Synthesis Markers in Diffuse Abscess Peritonitis, Thesis Ph.D., Medical University, Irkutsk (1998) (Russ.).
R. G. Saifutdinov, L. A. Sadochina and E. G. Grigojev, EPR study of MetHb in the peritonitis patient intestinal content, Rossiiskii Zhurnal Gastroenterologii, Gepatologii, Koloproktologii. 6:60 (1996) (Russ.).
R. G. Saifutdinov, L. A. Sadochina and E. G. Grigojev, Investigated of paramagnetic centres of the intestinal content by the method of ESR at the patients with the peritonitis, The Ninth Annual Conference of the International Society for Environmental Epidemiology, Academia Sinica International Center, Taiwan, Republic of China Taipei (1997), p. 242.
R. G. Saifutdinov, L. A. Sadochina and E. G. Grigojev, Paramagnetic centres of the intestinal content investigated by the method of the ESR at the patients with the peritonitis, Eighth International Conference on Bioinorganic Chemistry, 27 July–1 August, Japan, Yokohama, (1997), J. Inorganic. Biochem. 67: 132 (1997).
R. G. Saifutdinov, L. A. Sadokhina and E. G. Grigoriev, An EPR study of MetHb intestinal-content in peritonitic patients, International Workshop Fal’ka, June 20, Sankt-Peterburg (1996), p. 72.
R. G. Saifutdinov and L. A. Sadokhina, New aspects of endogenous intoxication in peritonitis, Rossiiskii Gastroenterologicheskii Zhurnal. N4: 131 (1997) (Russ.).
R. G. Saifutdinov, L. A. Sadochina and. G. Grigoriev, Application of EPR/ESR at prognosis of the course of peritonitis judging by the contents of methaemoglobin in the intestinal contents, The 4th Russia-Japan International Medical Symposium, September 3–8, Irkutsk (1996), pp. 28–29.
R. G. Saifutdinov, L. A. Sadochina and E. G. Grigoriev, Application of EPR/ESR at prognosis of the course of peritonitis judging by the contents of methaemoglobin in the intestinal contents, International Conference EPR-Spectroscopy of Nitric Oxide in Biological Systems, December 11–15, Suzdal (1996), pp. 28–29.
A. Ya. Lysenko and M. V. Pavlovskaya, SPID-Assotsiiruemye Infektsii i Invazii, Medicine, Moskva (1992) (Russ.).
A. E. Ades, C. F. Davison, F. J. Holland, D. M. Gibb, C. N. Hudson, A. Nicholl, G. D. Goldberg and C. S. Peckham, Vertically transmitted HIV infection in the British Isles, Brit. Med. J. 306: 1296 (1993).
L. M. Gordon, C. C. Curtain, Y. C. Zhong, A. Kirkpatrick, P. W. Mobley and A. J. Waring, The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation, Biochim. Biophys. Acta. 1139:257 (1992).
L. M. Gordon, C. C. Curtain, V. McCloyn, A. Kirkpatrick, P. W. Mobley and A. J. Waring, The amino-terminal peptide of HIV-1 gp41 interacts with human serum albumin, AIDS Res. Hum. Retroviruses. 9:1145 (1993).
Rights and permissions
Copyright information
© 2002 Kluwer Academic Publishers
About this chapter
Cite this chapter
(2002). Paramagnetic Centers in the Organism of Volunteers and Patients in Various Pathological States. In: Electron Paramagnetic Resonance in Biochemistry and Medicine. Topics in Applied Chemistry. Springer, Boston, MA. https://doi.org/10.1007/0-306-46925-1_3
Download citation
DOI: https://doi.org/10.1007/0-306-46925-1_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-46531-4
Online ISBN: 978-0-306-46925-1
eBook Packages: Springer Book Archive