Preview
Unable to display preview. Download preview PDF.
References
Adachi, O., Yamada, H.: Amine oxidases of microorganisms. VIII. Purification and properties of amine oxidase of Fusarium culmorum. Memoirs of the Research Institute for Food Science, Kyoto University 31, 10–18 (1970).
Adachi, O., Yamada, H., Ogata, K.: Purification and properties of putrescine oxidase of Micrococcus rubens. Agricult. biol. Chem. 30, 1202–1210 (1966).
Adler-Graschinsky, E., Langer, S. Z., Rubio, M. C.: Metabolism of norepinephrine released by phenoxybenzamine in isolated guinea-pig atria. J. Pharmacol. exp. Ther. 180, 286–301 (1972).
Alles, G. A., Heegaard, E. V.: Substrate specificity of amine oxidase. J. biol. Chem. 147, 487–503 (1943).
Argento-Ceru, M. P., Sartori, C., Aiutuori, F.: Diamine oxidase in rabbit liver. 1. Assay conditions and subcellular localization. Europ. J. Biochem. 34, 369–374 (1973a).
Argento-Ceru, M. P., Sartori, C., Aiutuori, F.: Diamine oxidase in rabbit liver. 2. Submicroscopial distribution. Europ. J. Biochem. 34, 375–382 (1973b).
Armstrong, M. D., McMillan, A., Shaw, K. N.: 3-Methoxy-4-hydroxy-D-mandelic acid, a urinary metabolite of norepinephrine. Biochim. biophys. Acta (Amst.) 25, 422–423 (1957).
Arunlakshana, O., Mongar, J. L., Schild, H. O.: Potentiation of pharmacological effects of histamine by histaminase inhibitors. J. Physiol. (Lond.) 123, 32–54 (1954).
AvakIan, V. M., Callingham, B. A.: An effect of adrenalectomy upon catecholamine metabolis. Brit. J. Pharmacol. 33, 211–212P (1968).
Avakian, O. V., Gillespie, J. S.: Uptake of noradrenaline by adrenergic nerves, smooth muscle and connective tissue in isolated perfused arteries and its correlation with the vasoconstrictor response. Brit. J. Pharmacol. 32, 168–184 (1968).
Axelrod, J.: The metabolism of catecholamines in vivo and in vitro. Pharmacol. Rev. 11, 402–408. (1959).
Bachrach, U.: Spermidine oxidase from Serratia marcescens. J. biol. Chem. 237, 3443–3448 (1962).
Bachrach, U.: Metabolism and function of spermine and related polyamines. Ann. Rev Microbiol. 24, 109–134 (1970).
Bailey, A. J., Fowler, L. J.: In vitro enzymic biosynthesis of two inter-chain crosslinks of bone collagen. Biochem. biophys. Res. Commun. 35, 672–675 (1969).
Bailey, A. J., Peach, C. M.: The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo. Biochem. J. 121, 257–259 (1971).
Bailey, A. J., Peach, C. M., Fowler, L. J.: Chemistry of the collagen cross-links. Isolation and characterization of two intermediate intermolecular cross-links in collagen. Biochem. J. 117, 819–831 (1970a).
Bailey, A. J., Peach, C. M., Fowler, L. J.: The biosynthesis of intermolecular cross-links in collagen. In: E. A. Balazs (Ed.): Chemistry and molecular biology of the intercellular matrix, Vol. 1, p. 385–404. London and New York: Academic Press 1970.
Banks, P., Mayor, D.: Intra-axonal transport in noradrenergic neurons in the sympathetic nervous system. Biochem. Soc. Symp. 36, 133–149 (1972).
Bardsley, W. G., Crabbe, M. J. C., Shindler, J. S.: Kinetics of the diamine oxidase reaction. Biochem. J. 131, 459–469 (1973).
Bardsley, W. G., Crabbe, M. J. C., Shindler, J. S., Ashford, J. S.: Oxidation of p-dimethylminomethylbenzylamine by pig kidney diamine oxidase. Biochem. J. 127, 875–879 (1972).
Bardsley, W. G., Hill, C. M., Lobley, R. W.: A reinvestigation of the substrate specificity of pig kidney diamine oxidase. Biochem. J. 117, 169–176 (1970).
Barker, D. L., Molinoff, P. B., Kravftz, E. A.: Octopamine in the lobster nervous system. Nature New Biology 236, 61–63 (1972).
Barlow, R. B., Blaschko, H., Himms, J. M., Trendelenburg, U.: Observations on ω-aminopolymethylene trimethylammonium compounds. Brit. J. Pharmacol. 10, 116–123 (1955).
Barnes, M. J., Constable, B. J., Morton, L. F., Kodicek, E.: Hydroxylysine in the N-terminal regions of the α1-and α2-chains of various collagens. Biochem. J. 125, 433–437 (1971).
Barondes, S. H.: On the site of synthesis of the mitochondrial protein of nerve endings. J. Neurochem. 13, 721–727 (1966).
Baudhuin, P., Beaufay, H., Rahman-Li, Y., Sellinger, O. Z., Wattiaux, R., Jacques, P., DeDuve, C.: Tissue fractionation studies 17. Intracellular distribution of monoamine oxidase, aspartate aminotransferase, alanine aminotransferase, D-amino acid oxidase and catalase in rat liver tissue. Biochem. J. 92, 179–184 (1964).
Baumgarten, H. G., Björklund, A., Lachenmayer, L., Nobin, A., Rosengren, E.: Evidence for the existence of serotonin-, dopamine-, and noradrenaline-containing neurones in the gut of Lampetra fluviatilis. Z. Zellforsch. 141, 33–54 (1973).
Baxter, R.: Origin and continuity of mitochondria. In: Origin and continuity of cell organelles (J. Reinert, H. Ursprung, Eds.), p. 46–64. Berlin-Heidelberg-New York: Springer 1971.
Baxter-Grillo, D. L.: Enzyme histochemistry and hormones of the developing gastrointestinal tract of the chick embryo III. Enterochromaffin cells—their possible products, glucagon, 5-hydroxytryptamine and the reaction of monoamine oxidase. Histochemie 21, 129–135 (1970).
Beattie, D. S.: Enzyme localization in the inner and outer membrane of rat liver mitochondria. Biochem. biophys. Res. Commun. 31, 901–907 (1968).
Beattie, D. S., Basford, R. E., Koritz, S. B.: The inner membrane as the site of the in vitro incorporation of L-[14C]leucine into mitochondrial protein. Biochemistry 6, 3099–3106 (1967).
Bertaccini, G.: Discussion Remark. In: Regional Neurochemistry (S. S. Kety, J. Elkes, Eds.), p. 305–306. Oxford-London-New York-Paris: Pergamon Press 1961.
Best, C. H.: The disappearance of histamine from autolysing lung tissue. J. Physiol. (Lond.) 67, 256–263 (1929).
Best, C. H., McHenry, E. W.: The inactivation of histamine. J. Physiol. (Lond.) 70, 349–372 (1930).
Black, J. W., Duncan, W. A. M., Durant, C. J., Ganellin, C. R., Parsons, E. M.: Definition and antagonism of histamine-H2 receptors. Nature 236, 385–390 (1972).
Blaschko, H.: The specific action of 1-dopa decarboxylase. J. Physiol. (Lond.) 96, 50–51P (1939).
Blaschko, H.: Amine oxidase in Sepia officinalis. J. Physiol. (Lond.) 99, 364–369 (1941).
Blaschko, H.: Amine oxidase and amine metabolism. Pharmacol. Rev. 4, 415–458 (1952a).
Blaschko, H.: Enzymic oxidation of 5-hydroxytryptamine in mammalian and cephalopod tissues. Biochem. J. 52, X (1952b).
Blaschko, H.: Oxidation of 1,4-methylhistamine by mammalian plasma. J. Physiol. (Lond.) 148, 570–573 (1959).
Blaschko, H.: Primary and secondary amines as substrates of amine oxidases. J. Physiol. (Lond.) 153, 17–18P (1960).
Blaschko, H.: The amine oxidases of mammalian blood plasma. Advances in comparative Physiology and Biochemistry 1, 67–116 (1962).
Blaschko, H.: Introduction and historical background. Advances in biochem. Psychopharmacol. 5, 1–10 (1972).
Blaschko, H.: Introductory remarks on monoamine oxidase. In: Catecholamines and their Enzymes in the Neuropathology of Schizophrenia (S. S. Kety, S. W. Matthysse, Eds.).In print.
Blaschko, H., Boadle, M. C.: Substrate specificity of amine oxidases. In: Pyridoxal Catalysis: Enzymes and Model Systems (Snell, E. E., Braunstein, A. E., Severin, E. S., Torchinsky, Yu. M., Eds.), p. 339–346. New York-London-Sydney: Interscience 1968.
Blaschko, H., Boadle, M. C., Strich, S. J.: Enzymic oxidation of amines in cyclostomes. J. Physiol. (Lond.) 204, 104–105P (1969).
Blaschko, H., Bonney, R.: Spermine oxidase and benzylamine oxidase. Distribution, development and substrate specificity. Proc. roy. Soc. B 156, 268–279 (1962).
Blaschko, H., Buffoni, F.: Pyridoxal phosphate as a constituent of the histaminase of pig plasma. Proc. roy. Soc. B 163, 45–60 (1965).
Blaschko, H., Buffoni, F., Weissman, N., Carnes, W. H., Coulson, W. F.: The amine oxidase of pig plasma in copper deficiency. Biochem. J. 96, 4C–5C (1965).
Blaschko, H., Chatterjee, M. L., Himms, J. M., Albert, A.: Enzymic oxidation of derivatives of ethylenediamine. Brit. J. Pharmacol. 10, 314–316 (1955).
Blaschko, H., Chrusciel, T. L.: Observations on the substrate specificity of amine oxidases. Brit. J. Pharmacol. 14, 364–367 (1959).
Blaschko, H., Colhoun, E. H., Frontali, N.: Occurrence of amine oxidase in an insect, Periplaneta americana L. J. Physiol. (Lond.) 156, 28P (1961).
Blaschko, H., Duthie, R.: Substrate specificity of amine oxidases. Biochem. J. 39, 478–481 (1945).
Blaschko, H., Hawes, R.: Observations on spermine oxidase of mammalian plasma. J. Physiol. (Lond.) 145, 124–131 (1959).
Blaschko, H., Hawkins, J.: Enzymic oxidation of aliphatic diamines. Brit. J. Pharmacol. 5, 625–632 (1950).
Blaschko, H., Hawkins, J.: Observations on amine oxidase in cephalopods. J. Physiol. (Lond.) 118, 88–93 (1952).
Blaschko, H., Hellmann, K.: Pigment formation from tryptamine and 5-hydroxytryptamine in tissues: a contribution to the histochemistry of amine oxidase. J. Physiol. (Lond.) 122, 419–427 (1953).
Blaschko, H., Himms, J. M.: Amine oxidase in the earthworm. J. Physiol. (Lond.) 120, 445–448 (1953).
Blaschko, H., Himms, J. M.: Enzymic oxidation in Decapods. J. exp. Biol. 31, 1–7 (1954).
Blaschko, H., Hope, D. B.: Observations on the distribution of amine oxidase in Invertebrates. Arch. Biochem. 69, 10–15 (1957).
Blaschko, H., Kirpekar, S. M., Phipps, S.: Observations on the enzymic oxidation of ω-amino acids. Arch. int. Pharmacodyn. 139, 120–122 (1962).
Blaschko, H., Kurzepa, S.: Potentiation of the response to histamine by picolylamines. Brit. J. Pharmacol. 19, 544–551 (1962).
Blaschko, H., Levine, W. G.: Metabolism of indolealkylamines. In: Handbuch der experimen-tellen Pharmakologie, Vol. 19 (V. Erspamer, Ed.), p. 212–244. Berlin-Heidelberg-New York: Springer 1965.
Blaschko, H., Richter, D., Schlossmann, H.: The inactivation of adrenaline. J. Physiol. (Lond.) 90, 1–19 (1937a).
Blaschko, H., Richter, D., Schlossmann, H.: The oxidation of adrenaline and other amines. Biochem. J. 31, 2187–2196 (1937b).
Bloom, F. E., Sims, K. L., Weitsen, H. A., Davis, G. A., Hanker, J. S.: Cytochemical differentiation between monoamine oxidase and other neuronal oxidases. Advances in biochem. Psychopharmacol. 5, 243–262 (1972).
Boadle, M. C.: A comparative study of amine oxidases. D. Phil. Thesis, Oxford 1967.
Boadle, M. C.: Observations on a histaminase of invertebrate origin: a contribution to the study of cephalopod amine oxidases. Comp. Biochem. Physiol. 30, 611–620 (1969).
Boadle, M. C., Blaschko, H.: Cockroach amine oxidase: classification and substrate specificity. Comp. Biochem. Physiol. 25, 129–138 (1968).
Boadle, M. C., Bloom, F. E.: A method for the fine structural demonstration of monoamine oxidase activity. J. Histochem. Cytochem. 17, 331–340 (1969).
Born, G. V. R.: 5-Hydroxytryptamine receptors. In: Smooth Muscle (Bülbring, E., Brading, A. F., Jones, A. W., Tomita, T., Eds.), p. 418–450. London: Arnold 1970.
Bornstein, P., Piez, K. A.: The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen. Biochemistry (Easton) 5, 3460–3473 (1966).
Brunner, G., Bygrave, F. L.: Microsomal marker enzymes and their limitations in distinguishing the outer membrane of rat liver mitochondria from the microsomes. Europ. J. Biochem. 8, 530–534 (1969).
Brunner, G., Neupert, W.: Turnover of outer and inner membrane proteins of rat liver mitochondria. FEBS Letters 1, 153–155 (1968).
Buffoni, F.: Histaminase and related amine oxidases. Pharmacol. Rev. 18, 1163–1199 (1966).
Buffoni, F.: Pyridoxal catalysis in pig plasma benzylamine oxidase (histaminase). In: Pyridoxal catalysis: Enzymes and model systems (Snell, E. E., Braunstein, A. E., Severin, E. S., Torchinsky, Yu. M., Eds.), p. 363–374. New York-London-Sydney: Interscience 1968.
Buffoni, F., Blaschko, H.: Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma. Proc. roy. Soc. B 161, 153–167 (1964).
Buffoni, F., Della Corte, L.: Pig plasma benzylamine oxidase. Advances in biochem. Psycho-pharmacol. 5, 133–149 (1972).
Buffoni, F., Della Corte, L., Ignesti, G.: Pig plasma benzylamine oxidase (histaminase): Kinetic studies. Pharmacol. Res. Commun. 4, 99–122 (1972).
Buffoni, F., Della Corte, L., Knowles, P. F.: The nature of copper in pig plasma benzylamine oxidase. Biochem. J. 106, 575–576 (1968).
Burkard, W. P., Gey, K. F., Pletscher, A.: A new inhibitor of decarboxylase of aromatic amino acids. Experientia (Basel) 18, 411–412 (1962).
Burkard, W. P., Gey, K. F., Pletscher, A.: Diamine oxidase in the brain of vertebrates. J. Neurochem. 10, 183–186 (1963).
Burn, J. H.: The enzyme at sympathetic nerve endings. Brit. med. J. 1952 I, 784–785.
Bygrave, F. L., Bücher, Th.: Synthesis in vivo of the lecithin component of the inner and outer membranes of rat liver mitochondria. FEBS Letters 1, 42–45 (1968).
Caesar, P. M., Collins, G. G. S., Sandler, M.: Catecholamine metabolism and monoamine oxidase activity in adrenalectomized rats. Biochem. Pharmacol. 19, 921–926 (1970).
Callingham, B. A., Della Corte, L.: Effect of adrenalectomy upon some rat heart enzymes. Brit. J. Pharmacol. 41, 392P (1971).
Callingham, B. A., Della Corte, L.: The influence of growth and of adrenalectomy upon some rat heart enzymes. Brit. J. Pharmacol. 46, 530–531 (1972).
Campello, A. P., Tabor, C. W., Tabor, H.: Resolution of spermidine dehydrogenase from Serratia marcescens: requirements for flavin adenin dinucleotide and an additional electron carrier. Biochem. biophys. Res. Commun. 19, 6–9 (1965).
Carlsson, A.: Pharmacological depletion of catecholamine stores. Pharmacol. Rev. 18, 541–549 (1966).
Carlsson, A., Bédard, P., Lindqvist, M., Magnusson, T.: The influence of nerve-impulse flow on the synthesis and metabolism of 5-hydroxytryptamine in the central nervous system. Biochem. Soc. Symp. 36, 17–32 (1972).
Carlsten, A.: Effect of adrenalectomy on lymph and plasma histaminase. Acta physiol. scand. 20, suppl. 70, 33–46 (1950).
Carnes, W. H.: Copper and connective tissue metabolism. International Review of Connective Tissue Research 4, 197–232 (1968).
Carnes, W. H.: Role of copper in connective tissue metabolism. Fed. Proc. 30, 995–1000 (1971).
Chaudhary, K. D., Srivastava, U., Lemonde, J. A.: Monoamine oxidase in Tribolium confusum Duval (Coleoptera). Biochim. biophys. Acta (Amst.) 132, 290–299 (1967).
Code, C. F., Cody, D. T., Hurn, M., Kennedy, J. C., Strickland, M.: The simultaneous release of histamine and a histamine-destroying factor during anaphylaxis in rats. J. Physiol. (Lond.) 156, 207–216 (1961).
Collins, G. G. S., Sandler, M.: Human blood platelet monoamine oxidase. Biochem. Pharmacol. 20, 289–296 (1971).
Consolo, S., Giacobini, E., Karjalainen, K.: Monoamine oxidase: sympathetic ganglia of the cat. Acta physiol. scand. 74, 513–520 (1968).
Costa, E., Sandler, M. (Eds.): Monoamine oxidases — new vistas. Advances in biochem. Psychopharmacol. 5, 1–454 (1972).
Costa, T. M., Rotilio, G., Finazzi-Agro, A., Vallogini, M. P., Mondovi, B.: On the active site of diamine oxidase: kinetic studies. Arch. Biochem, 147, 8–13 (1971).
Cotzias, G. L., Dole, V. P.: Metabolism of amines II. Mitochondrial localization of monoamine oxidase. Proc. Soc. exp. Biol. (N.Y.) 78, 157–160 (1951).
Dahlbäck, O., Hansson, R., Tibbling, G., Tryding, N.: The effect of heparin on diamine oxidase and lipoprotein lipase in human lymph and blood plasma. Scand. J. clin. Lab. Invest. 21, 17–25 (1968).
Dahlström, A.: Axoplasmic transport (with particular respect to adrenergic neurons). Phil. Trans. B 261, 325–358 (1971).
Dahlström, A.: The axonal transport of monoamine oxidases. Advances in biochem. Psychopharmacol. 5, 293–305 (1972).
De la Lande, I. S., Jellett, L. B.: Relationship between the roles of monoamine oxidase and sympathetic nerves in the vasoconstrictor response of the rabbit ear artery to norepinephrine. J. Pharmacol. exp. Ther. 180, 47–55 (1972).
Della Corte, L., Perrino, I.: Il ruolo delle aminossidasi plasmatiche nel metabolismo della dopamina. Farmaco, Ed. sci. 23, 204–209 (1968).
De Sa, R. J.: Putrescine oxidase from Micrococcus rubens, Purification and properties of the enzyme. J. biol. Chem. 247, 5527–5534 (1972).
Draskoczy, P. R., Trendelenburg, U.: Intraneuronal and extraneuronal accumulation of sympathomimetic amines in the isolated nictitating membrane of the cat. J. Pharmacol. exp. Ther. 174, 290–306 (1970).
Eady, R. R., Jarman, T. R., Large, P. J.: Microbial oxidation of amines. Partial purification of a mixed-function secondary amine oxidase system from Pseudomonas aminovorans that contains an enzymically active cytochrome—P-420-type haemoprotein. Biochem. J. 125, 449–459 (1971).
Eady, R. R., Large, P. J.: Microbial oxidation of amines. Spectral and kinetic properties of primary amine dehydrogenase of Pseudomonas AM1. Biochem. J. 123, 757–771 (1971).
Ehinger, B., Falck, B.: Concomitant adrenergic and parasympathetic fibres in the rat iris. Acta physiol. scand. 67, 201–207 (1966).
Ehinger, B., Falck, B., Rosengren, A.-M., Sporrong, B.: Acetylcholine in adrenergic nerve terminals of the cat iris. J. Physiol. (Lond.) 209, 557–565 (1970).
Eiduson, S.: Ontogenetic development of monoamine oxidase. Advances in biochem. Psychopharmacol. 5, 271–287 (1972).
EiseNfeld, A. J., Axelrod, J., Krakoff, L.: Inhibition of the extraneuronal accumulation and metabolism by adrenergic blocking agents. J. Pharmacol. exp. Ther. 156, 107–113 (1967a).
Eisenfeld, A. J., Landsberg, L., Axelrod, J.: Effect of drugs on the accumulation and metabolism of extraneuronal norepinephrine in the rat heart. J. Pharmacol. exp. Ther. 158, 378–385 (1967b).
Eliassen, K. A.: Metabolism of 14C-histamine in goats and pigs treated with aminoguanidine. Acta physiol. scand. 88, 1–7 (1973).
Eränkö, L., Eränkö, O.: Effect of hydrocortisone on histochemically demonstrable catecholamines in the sympathetic ganglia and extraneuronal chromaffin tissue of the rat. Acta physiol. scand. 84, 125–133 (1972).
Eränkö, O., Eränkö, L., Hill, C. E., Burnstock, G.: Hydrocortisone-induced increase in the number of small intensely fluorescent cells and the histochemically demonstrable catecholamine contact in cultures of sympathetic ganglia of the rat. Histochem. J. 4, 49–58 (1972).
Erspamer, V.: Identification of octopamine as 1-p-hydroxy-phenylethanolamine. Nature (Lond.) 169, 800–801 (1952).
Erwin, V. G., Hellerman, L.: Mitochondrial monoamine oxidase I. Purification and characterization of the bovine kidney enzyme. J. biol. Chem. 242, 4230–4238 (1967).
Erwin, V. G., Simon, R. J.: Occurrence of newly synthesized monoamine oxidase in subcellular fractions of the rat liver. J. pharm. Sci. 58, 1033–1035 (1969).
Finazzi-Agro, A., Rotilio, G., Costa, T. M., Mondovi, B.: Evidence for a ping-pong mechanism in the diamine oxidase reaction. FEBS Letters 4, 31–32 (1969).
Fischer, J. E., Kopin, I. J., Axelrod, J.: Evidence for extraneuronal binding of norepinephrine. J. Pharmacol. exp. Ther. 147, 181–185 (1965).
Fowler, L. J., Peach, C. M., Bailey, A. J.: In vitro studies on the enzymic biosynthesis of the collagen crosslinks. Biochem. biophys. Res. Commun. 41, 251–259 (1970).
Franzblau, C., Faris, B., Lent, R. W., Salcedo, L. L., Smith, B., Jaffe, R., Crombie, G.: Chemistry and biosynthesis of crosslinks in elastin. In: Chemistry and Molecular Biology of the Intercellular Matrix (Balazs, E. A., Ed.), Vol. I, p. 617–639. London-New York: Academic Press 1970.
Franzblau, C., Sinex, F. M., Faris, B., Lampidis, R.: Identification of a new crosslinking amino acid in elastin. Biochem. biophys. Res. Commun. 21, 575–581 (1965).
Freyburger, W. A., Graham, B. E., Rapport, M. M., Seay, P. H., Govier, W. M., Swoap, O. F., van der Brook, M. J.: tJ. Pharmacol. exp. Ther. 55, 80–86 (1952).
Fujiwara, M., Tanaka, C., Hikosaka, H., Okegawa, T.: Cytological localization of nor-adrenaline, monoamine oxidase and acetylcholinesterase in salivary glands of dog. J. Histo-chem. Cytochem. 14, 483–490 (1966).
Fuller, R. W.: Selective inhibition of monoamine oxidase. Advances in biochem. Psycho-pharmacol. 5, 339–354 (1972).
Furness, J. B., Costa, M.: Monoamine oxidase histochemistry of enteric neurones in the guinea pig. Histochemie 28, 324–336 (1971).
Furness, J. B., Costa, M.: The nervous release and the action of substances which affect intestinal muscle through neither adrenoreceptors nor cholinoreceptors. Phil. Trans. B 265, 123–133 (1973).
Fuxe, K., Hökfelt, T., Ungerstedt, U.: Localization of indolealkylamine in CNS. Advances Pharmacol. 6A, 235–251 (1968).
Gallop, P. M., Blumenfeld, O. O., Henson, E., Schneider, A. L.: Isolation and identification of α-amino-aldehydes in collagen. Biochemistry 7, 2409–2430 (1968).
Gallop, P. M., Blumenfeld, O. O., Paz, M. A.: Aldehydes and aldehyde derivatives in collagen. In: Chemistry and molecular biology of the intercellular matrix (Balazs, E. A., Ed.), Vol. 1, p. 179–194. London-New York: Academic Press 1970.
Gear, A. R. L.: Inner-and outer-membrane enzymes of mitochondria during liver regeneration. Biochem. J. 120, 577–587 (1970).
Ghisla, S., Hemmerich, P.: Synthesis of the flavocoenzyme of monoamine oxidase. FEBS Letters 16, 229–232 (1971).
Giacobini, E., Kerpel-Fronius, S.: Histochemical and biochemical correlations of monoamine oxidase activity in autonomic and sensory ganglia of the cat. Acta physiol. scand. 78, 522–528 (1970).
Gillespie, J. S., Hamilton, D. N. H., Hosie, R. J. A.: The extraneuronal uptake and localization of noradrenaline in the cat spleen and the effect on this of some drugs, of cold and of denervation. J. Physiol. (Lond.) 206, 563–590 (1970).
Gillespie, J. S., Muir, T. C.: Species and tissue variation in extraneuronal and neuronal accumulation of noradrenaline. J. Physiol. (Lond.) 206, 591–604 (1970).
Glenner, G. G., Burtner, H. J., Brown, G. W., Jr.: The histochemical demonstration of monoamine oxidase activity by tetrazolium salts. J. Histochem. Cytochem. 5, 591–600 (1957).
Gomes, B., Igaue, I., Kloepfer, H. G., Yasunobu, K. T.: Amine oxidase XIV. Isolation and characterization of the multiple forms of beef liver amine oxidase components. Arch. Biochem. 132, 16–27 (1969).
Goridis, C., Neff, N. H.: Evidence for a specific monoamine oxidase associated with sympathetic nerves. Neuropharmacology 10, 557–564 (1971a).
Goridis, C., Neff, N. H.: Monoamine oxidase in sympathetic nerves: a transmitter specific enzyme type. Brit. J. Pharmacol. 43, 814–818 (1971b).
Gorkin, V. Z.: Qualitative alterations in enzymatic properties of amine oxidases. Advances in biochem. Psychopharmacol. 5, 55–65 (1972).
Gorkin, V. Z., Gridneva, L. I., Romanova, L. A., Severina, I. S.: Spectrophotometric determination of monoamine oxidase activity in mitochondria. Biochemistry 27, 852–860 (1962).
Goryachenkova, E. V., Sherbatiuk, L. I., Zamaraev, C. I.: Purification of pig kidney diamine oxidase and an investigation of the nature of its prosthetic groups. In: Pyridoxal Catalysis: Enzymes and model systems (Snell, E. E., Braunstein, A. E., Severin, E. S., Torchinsky, Yu. M., Eds.), p. 391–402. New York-London-Sydney: Interscience 1968.
Hagen, P., Weiner, N.: Enzymic oxidation of pharmacologically active amines. Fed. Proc. 18, 1005–1012 (1959).
Hakanson, R., Owman, C.: Pineal decarboxylase and monoamine oxidase activities as related to the monoamine stores. J. Neurochem. 13, 597–605 (1966).
Hamilton, G. A.: A possible model reaction for pyridoxal phosphate dependant amine oxidases. In: Pyridoxal catalysis: Enzymes and model systems (Snell, E. E., Braunstein, A. E., Severin, E. S., Torchinsky, Yu. M., Eds.), p. 375–390. New York-London-Sydney: Interscience 1968.
Hanker, J. S., Kusyk, C. J., Bloom, F. E., Pearse, A. G. E.: The demonstration of dehydrogenases and monoamine oxidase by the formation of osmium blacks at the sites of Hatchett's brown. Histochemie 33, 205–230 (1973).
Hannonen, P., Jänne, J., Raina, A.: Partial purification and characterization of spermine synthase from rat brain. Biochim. biophys. Acta (Amst.) 289, 225–231 (1972a).
Hannonen, P., Raina, A., Jänne, J.: Polyamine synthesis in the regenerating rat liver: stimulation of S-adenosyl-methionine decarboxylase and spermidine and spermine syntheses after partial hepatectomy. Biochim. biophys. Acta (Amst.) 273, 84–90 (1972b).
Hansson, R., Thysell, H.: Diamine oxidase in blood plasma in some vertebrates and Anodonta cygnea before and after injection of heparin. Acta physiol. scand. 74, 533–542 (1968).
Hare, M. L. C.: Tyramine oxidase. I. A new enzyme system in liver. Biochem. J. 22, 968–979 (1928).
Harris, E. D., Gonnerman, W. A., O'Dell, B. L.: Purification properties of chick aorta lysyl oxidase. Fed. Proc. 32, 594 (1973).
Harris, E. D., O'Dell, B. L.: Comparison of soluble and particulate amine oxidases from bovine aorta. Biochim. biophys. Res. Commun. 48, 1173–1178 (1972).
Hartman, B. K., Udenfriend, S.: The use of immunological techniques for the characterization of bovine monoamine oxidase from liver and brain. Advances in biochem. Psychopharmacol. 5, 119–128 (1972).
Hartman, B. K., Yasunobu, K. T., Udenfriend, S.: Immunological identity of the multiple forms of beef liver mitochondrial monoamine oxidase. Arch. Biochem. 147, 797–804 (1971).
Hawkins, J.: The localization of amine oxidase in the liver cell. Biochem. J. 50, 577–581 (1952a).
Hawkins, J.: Amine oxidase activity of rat liver in riboflavin deficiency. Biochem. J. 51, 399–404 (1952b).
Hawkins, J., Walker, J. M.: The effect of colchicine on the enzyme content of regenerating rat liver and on the pressor amine content of the adrenal. Brit. J. Pharmacol. 7, 152–160 (1952).
Hayes, D. K., Wash, D. B., Odesser, D. B., Schechter, M. S.: Phosphodiesterase and monoamine oxidase in larvae of the European corn borer exposed to two photoperiodic regimes. Fed. Proc. 30, 1268 Abs (1971).
Hayes, D. K., Wash, D. B., Schechter, M. S.: Monoamine oxidase activity in larvae of the European corn borer. J. econ. Entomol. 65, 1229–1232 (1972).
Hellerman, L., Chuang, H. Y. K., De Luca, D. C.: Approaches to the catalytic mechanism of mitochondrial monoamine oxidase. Adv. biochem. Psychopharmacol. 5, 327–337.
Henze, M.: p-Oxyphenyläthylamin, das Speicheldrüsengift der Cephalopoden. Hoppe-Seylers Z. physiol. Chem. 87, 51–58 (1913).
Hidaka, H., Hartman, B., Udenfriend, S.: Comparison of mitochondrial monoamine oxidases from bovine brain and liver using antibody to purified liver monoamine oxidase. Arch. Biochem. 147, 805–809 (1971).
Hill, C. H., Kim, C. S.: The derangement of elastin synthesis in pyridoxine deficiency. Biochem. biophys. Res. Commun. 27, 94–99 (1967).
Hill, J. M., Mann, P. J. G.: The inhibition of pea-seedling diamine oxidase by chelating agents. Biochem. J. 85, 198–207 (1962).
Hill, J. M., Mann, P. J. G.: Further properties of the diamine oxidase of pea seedlings. Biochem. J. 91, 171–182 (1964).
Hökfelt, T.: Electron microscopic observations on nerve terminals in the intrinsic muscles of the albino rat iris. Acta physiol. scand. 67, 255–256 (1966).
Hökfelt, T., Jonsson, G.: Studies on reaction and binding of monoamines after fixation and processing for electron microscopy with special reference to fixation with potassium permanganate. Histochemie 16, 45–67 (1966).
Holtz, P., Heise, R., Lüdtke, K.: Fermentativer Abbau von 1-Dioxyphenylalanin (Dopa) durch Niere. Naunyn-Schmiedebergs Arch. Pharmak. exp. Path. 191, 87–118 (1938).
Holtz, P., Palm, D.: Brenzkatechinamine und andere sympathicomimetische Amine. Ergebn. Physiol. 58, 1–580 (1966).
Holtz, P., Stock, K., Westermann, E.: Pharmakologie des Tetrahydropapaverolins und seine Entstehung aus Dopamin. Naunyn-Schmiedeberg's Arch. Pharmak. exp. Path. 248, 387–405 (1964).
Hope, D. B.: The metabolism of taurine and related compounds. D. Phil. Thesis, Oxford 1956.
Hope, D. B., Smith, A. D.: Distribution and activity of monoamine oxidase in mouse tissues. Biochem. J. 74, 101–107 (1960).
Horita, A., Lowe, M. C.: On the extraneuronal nature of cardiac monoamine oxidase in the rat. Advances in biochem. Psychopharmacol. 5, 227–242 (1972).
Houslay, M. D., Tipton, K. F.: The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase. Biochem. J. 135, 173–186 (1973).
Ho-Van-Hap, A., Babineau, L. M., Berlinguet, L.: Hormonal action on monoamine oxidase activity in rats. Canad. J. Biochem. 45, 355–362 (1967).
Huikuri, K. T.: Histochemistry of the ciliary ganglion of the rat and the effect of pre-and postganglionic nerve division. Acta physiol. scand. 69, suppl. 286, 1–83 (1966).
Hunter, N. W.: Intracellular localization of some hydrolases, and iron and copper porphyric enzymes in Opalina carolinensis. Trans. Amer. Microscop. Soc. 76, 36–45 (1957).
Hunter, N. W.: Enzyme patterns in Paramecium putrinum Claparède and Lachmann. Trans. Amer. Microscop. Soc. 78, 363–370 (1959a).
Hunter, N. W.: Enzyme systems of Stylonychia pustulata II. Miscellaneous systems (hydrases, hydrolases and dehydrogenases). Protozool. 6, 100–104 (1959b).
Hunter, N. W.: Enzyme systems of Colpoda cucullus. II. Intracellular activity of some enzymes as determined by histochemistry. Trans. Amer. Microscop. Soc. 80, 38–43 (1961).
Igaue, I., Gomes, B., Yasunobu, K. T.: Beef mitochondrial monoamine oxidase, a flavin dinucleotide enzyme. Biochem. biophys. Res. Commun. 29, 562–570 (1967).
Iversen, L. L.: The uptake and storage of noradrenaline in sympathetic nerves. Cambridge: University Press 1967.
Iversen, L. L.: Role of transmitter uptake mechanisms in synaptic neurotransmision. Brit. J. Pharmacol. 41, 571–591 (1971).
Iwata, H., Kariya, K.: Adrenergic mechanisms in Tetrahymena. I. Changes in monoamine oxidase activity during growth. Experientia (Basel) 29, 265–266 (1973).
Iwata, H., Kariya, K., Okamoto, H.: Amine oxidative system in Tetrahymena pyriformis W. Experientia (Basel) 27, 388–390 (1971).
Janakidevi, K., Dewey, V. C., Ktdder, G. W.: The biosynthesis of catecholamines in two genera of protozoa. J. biol. Chem. 241, 2576–2578 (1966).
Jarrott, B.: Occurrence and properties of monoamine oxidase in adrenergic neurons. J. Neurochem. 18, 7–16 (1971).
Jarrott, B., Iversen, L. L.: Subcellular distribution of monoamine oxidase activity in rat liver and vas deferens. Biochem. Pharmacol. 17, 1619–1625 (1968).
Jarrott, B., Iversen, L. L.: Noradrenaline metabolizing enzymes in normal and sympathetically denervated vas deferens. J. Neurochem. 18, 1–6 (1971).
Johnston, J. P.: Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem. Pharmacol. 17, 1285–1297 (1968).
Jonason, J.: Metabolism of catecholamines in the central and peripheral nervous system. A study with special reference to the enzymes involved. Acta physiol. scand. Suppl. 320, 1–50 (1969).
Kahlson, G., Rosengren, E.: Biogenesis and physiology of histamine. Monograph No. 21 of the Physiol. Soc. London: Arnold 1971.
Kaiser, W., Bygrave, F. L.: Incorporation of choline into the outer and inner membranes of isolated rat liver mitochondria. J. Biochem. 4, 582–585 (1968).
Kalsner, S., Nickerson, M.: A method for the study of mechanisms of drug disposition in smooth muscle. Canad. J. Physiol. Pharmacol. 46, 719–730 (1968).
Kalsner, S., Nickerson, M.: Mechanisms of cocaine potentiation of responses to amines. Brit. J. Pharmacol. 35, 428–439 (1969a).
Kalsner, S., Nickerson, M.: Effects of a haloalkylamine on responses to a disposition of sympathomimetic amines. Brit. J. Pharmacol. 35, 440–455 (1969b).
Kapeixer-Adler, R.: Amine oxidases and methods for their study, p. 1–319. New York-London-Sydney-Toronto: Wiley-Interscience 1970.
Kapeixer-Adler, R., Iggo, B.: Histamine and its derivatives in human urine. Biochim. biophys. Acta (Amst.) 25, 394–402 (1957).
Karlsson, J.-O., Sjöstrand, J.: Synthesis, migration and turnover of protein in retinal ganglion cells. J. Neurochem. 18, 749–767 (1971).
Kearney, E. B., Salach, J. I., Walker, W. H., Seng, R. L., Kenney, W., Zeszotek, E., Singer, T. P.: The covalently-bound flavin of hepatic monoamine oxidase. 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8a position. Europ. J. Biochem. 24, 321–327 (1971).
Kim, C. S., Hill, C. H.: The interrelationship of dietary copper and amine oxidase in the formation of elastin. Biochem. biophys. Res. Commun. 24, 395–400 (1966).
Kim, H. C., D'Iorio, A.: Possible isoenzymes of monoamine oxidase in rat tissues. Canad. J. Biochem. 46, 295–297 (1968).
Koelle, G. B., Valk, A. de T., Jr.: Physiological implications of the histochemical localization of monoamine oxidases. J. Physiol. (Lond.) 126, 434–447 (1954).
Kohn, H. I.: Tyramine oxidase. Biochem. J. 31, 1693–1704 (1937).
Kopin, I. J.: Storage and metabolism of catecholamines: The role of monoamine oxidase. Pharmacol. Rev. 16, 179–191 (1964).
Kreutzberg, G. W.: Neuronal dynamics and axonal flow IV. Blockage of intra-axonal enzyme transport by colchicine. Proc. nat. Acad. Sci. (Wash.) 62, 722–728 (1969).
Kumagai, H., Matsui, H., Ogata, K., Yamada, H.: Properties of crystalline tyramine oxidase from Sarcina lutea. Biochim. biophys. Acta (Amst.) 171, 1–8 (1969a).
Kumagai, H., Matsui, H., Ogata, K., Yamada, H., Fukami, H.: Oxidation of dopamine by crystalline tyramine oxidase from Sarcina lutea. Memoirs of the Research Institute for Food Science, Kyoto University, No. 29, 69–71 (1968).
Kumagai, H., Nagate, T., Yamada, H., Fukami, H.: Characterization of sodium borohydride-reduced histaminase-histamine intermediate. Biochim. biophys. Acta (Amst.) 185, 242–244 (1969b).
Kumagai, H., Yamada, H., Suzuki, H., Ogura, Y.: Action mechanism of tyramine oxidase from Sarcina lutea. J. Biochem. 69, 137–144 (1971).
Kuttan, R., Radhakrishnan, A. N.: Studies on the biosynthesis of syw-homospermidine in sandal (Santalum album L.). Biochem. J. 127, 61–67 (1972).
Kveder, S., Iskric, S., Keglevic, D.: 5-hydroxytryptophol: a metabolite of 5-hydroxytryptamine in rats. Biochem. J. 85, 447–449 (1962).
Lake, C. R., Mills, R. R., Burnet, P. C. J.: β-hydroxylation of tyramine by cockroach hemolymph. Biochim. biophys. Acta (Amst.) 215, 226–228 (1970).
Lehmann, G., Randall, L. O.: Pharmacological properties of sympathomimetic diamines. J. Pharmacol. exp. Ther. 93, 114–125 (1948).
Lempinen, M.: Extra-adrenal chromaffin tissue of the rat and the effect of cortical hormones on it. Acta physiol. scand. 62, suppl. 231, 1–91 (1964).
Lent, R., Franzblau, C.: Studies on the reduction of bovine elastin: Evidence for the presence of Δ6,7-dehydrolysinonorleucine. Biochem. biophys. Res. Commun. 26, 43–50 (1967).
Levene, C. I.: The lathyrogenic effect of isonicotonic acid hydrazide (INAH) on the chick embryo and its reversal by pyridoxal. J. exp. Med. 113, 795–810 (1961).
Levene, C. I.: Studies on the mode of action of lathyrogenic compounds. J. exp. Med. 116, 119–130 (1962).
Levene, C. I.: Effect of lathyrogenic compounds on the cross-linking of collagen and elastin in vivo. In: A Symposium on mechanisms of toxicity (Aldrtdge, E., Ed.), p. 67–85. London: Macmillan 1971.
Levene, C. I., Gross, J.: Alterations in state of molecular aggregation of collagen induced in chick embryos by β-aminopropionitrile (lathyrus factor). J. exp. Med. 110, 771–790 (1959).
Lightman, S. L., Iversen, L. L.: The role of uptake 2 in the extraneuronal metabolism of catecholamines in the isolated rat heart. Brit. J. Pharmacol. 37, 638–649 (1969).
Lindell, S.-E., Westling, H.: Enzymic oxidation of some substances related to histamine. Acta physiol. scand. 39, 370–384 (1957).
Lindström, A., Olsson, B., Pettersson, G.: Kinetics of the interaction between pig plasmabenzylamine oxidase and substrate. Europ. J. Biochem. 35, 70–77 (1973).
Lindström, A., Olsson, B., Pettersson, G.: Transient kinetics of benzaldehyde formation during the catalytic action of pig-plasma benzylamine oxidase. Europ. J. Biochem. 42, 377–382 (1974).
Lindström, A., Pettersson, G.: Active-site titration of pig plasma benzylamine oxidase with hydrazine derivatives. Europ. J. Biochem. 34, 564–568 (1973).
Lovenberg, W., Dixon, E., Keiser, H. R., Sjoerdsma, A.: A comparison of amine oxidase activity in human skin and rat liver: relevance to collagen cross-linking. Biochem. Pharmacol. 17, 1117–1120 (1968).
McCaulay, R., Racker, E.: Separation of two monoamine oxidases from bovine brain. Fed. Proc. 32, 797 Abst. (1973).
McEwen, C. M.: Human plasma monoamine oxidase. I. Purification and identification. J. biol. Chem. 240, 2003–2010 (1965).
McEwen, C. M.: The soluble monoamine oxidase of human plasma and sera. Advances in biochem. Psychopharmacol. 5, 157–165 (1972).
McLean, J. R., Burnstock, G.: Axoplasmic flow of adrenaline and monoamine oxidase in amphibian sympathetic nerves. Z. Zellforsch. 124, 44–56 (1972).
Mann, P. J. G.: Further purification and properties of the amine oxidase of pea seedlings. Biochem. J. 79, 623–631 (1961).
Martin, G. R., Pinnell, S. R., Siegal, R. C., Goldstein, E. R.: Lysyl oxidase: The enzymatic step in collagen and elastin cross-linking. In: Chemistry and molecular biology of the intercellular matrix (Balazs, E. A., Ed.), Vol. I, p. 405–410. London and New York: Academic Press 1970.
Medical Research Council: Biochemical research in psychiatry: survey and proposals. Report by a Council Committee, p. 11. London: Her Majesty's Stationery Office: 1970.
Mondovi, B.: On the mechanism of amine oxidation by diamine oxidases. Advances in biochem. Psychopharmacol. 5, 181–183 (1972).
Mondovi, B., Costa, M. T., Finazzi-Agro, A., Rotilio, G.: Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase. Arch. Biochem. 119, 373–381 (1967a).
Mondovi, B., Rotilio, G., Costa, M. T., Finazzi-Agro, A., Chiancone, E., Hansen, R. E., Beinert, H.: Diamine oxidase of pig kidney. Improved purification and properties. J. biol. Chem. 242, 1160–1167 (1967b).
Mondovi, B., Rotilio, G., Finazzi-Agro, A., Vallogini, M. P., Malmström, B. G., Antonini, E.: Copper reduction by substrate in diamine oxidase. FEBS Letters 2, 182–184 (1969).
Müller, E., Pearse, A. G. E.: Localization of monoamine oxidase in mammalian and reptilian heart. Brit. Heart J. 27, 116–120 (1965).
Nagatsu, T., Nakano, G., Mizutani, K., Harada, M.: Purification and properties of amine oxidases in brain and connective tissue (dental pulp). Advances in biochem. Psychopharmacol. 5, 25–36 (1972).
Narayanan, A. S., Siegel, R. C., Martin, G. R.: On the inhibition of lysyl oxidase by β-aminopropionitrile. Biochem. biophys. Res. Commun. 46, 745–751 (1972).
Neff, N. H., Goridis, C.: Neuronal monoamine oxidase: specific enzyme types and their rates of formation. Advances in biochem. Psychopharmacol. 5, 307–323 (1972).
Neupert, W., Brdiczka, D., Bücher, Th.: Incorporation of amino acids into the outer and inner membrane of isolated rat liver mitochondria. Biochem. biophys. Res. Commun. 27, 488–493 (1967).
Neupert, W., Brdiczka, D., Sebald, W.: Incorporation of amino acids in the outer and inner membrane of isolated rat liver mitochondria. In: Biochemical aspects of the biogenesis of mitochondrial (Slater, E. C., Tager, M., Papa, S., Quagliarello, E., Eds.), p. 395–408. Bari: Adriatica 1968.
Nimmo-Smith, R. H., Raison, C. G.: Monoamine oxidase activity of Schistosoma mansoni. Comp. Biochem. Physiol. 24, 403–416 (1968).
Nimni, M. E., Deshmukh, K., Deshmukh, A.: Mechanism of inhibition of collagen cross-linking and depolymerization of an incompletely crosslinked form of insoluble collagen caused by D-penicillamine. In: Chemistry and Molecular Biology of the Intercellular Matrix (Balazs, E. A., Ed.), p. 417–430. London-New York: Academic Press 1970.
Nimni, M. E., Deshmukh, K., Gerth, N.: Collagen defect induced by penicillamine. Nature New Biology 240, 220–221 (1972).
Novick, W. J.: The effect of age and thyroid hormones on the monoamine oxidase of rat heart. Endocrinology 69, 55–59 (1961).
O'Deix, B. L., Hardwick, B. C., Reynolds, G., Savage, J. E.: Connective tissue defect in the chick resulting from copper deficiency. Proc. Soc. exp. Biol. (N.Y.) 108, 402–404 (1961).
Okamoto, H.: Influence of L-thyroxine on kynurenine 3-hydroxylase, monoamine oxidase, and rotenone-insensitive NADH-cytochrome C reductase in mitochondrial outer membrane. Biochem. biophys. Res. Commun. 43, 827–833 (1971).
Okamoto, H., Yamamoto, S., Nozaki, M., Hayaishi, O.: On the submitochondrial localization of L-kynurenine-5-hydroxylase. Biochem. biophys. Res. Commun. 26, 309–314 (1967).
Ouvecrona, T., Oreland, L.: Reassociation of soluble monoamine oxidase with lipid-depleted mitochondria in the presence of phospholipids. Biochemistry 10, 332–340 (1971).
Oreland, L.: Purification and properties of pig liver mitochondrial monoamine oxidase. Arch. Biochem. 146, 410–421 (1971).
Oreland, L.: Some properties of pig liver mitochondrial monoamine oxidase. Advances in biochem. Psychopharmacol. 5, 37–43 (1972).
Oreland, L., OLIvecrona, T.: The role of acidic phospholipids in the binding of monoamine oxidase to the mitochondrial structure. Arch. Biochem. 142, 710–714 (1971).
Paasonen, M. K.: Inactivation of 5-hydroxytryptamine by mammalian blood platelets. Biochem. Pharmacol. 8, 241–244 (1961).
Padmanabhan, R., Kim, K. H.: Oxidation of spermidine by a Pseudomonas. Biochem. biophys. Res. Commun. 19, 1–5 (1965).
Page, R. C., Benditt, H. E. P.: Interaction of the lathyrogen beta-aminopropionitrile (BAPN) with a copper-containing amine oxidase. Proc. Soc. exp. Biol. (N.Y.) 124, 454–459 (1967).
Paolucci, F., Cronenberger, L., Plan, R., Pacheco, H.: Purification et propriétés de la diamine: oxygène oxydo-reductase du placenta humain. Biochimie 53, 735–749 (1971).
Pare, C. M. B.: Clinical implications of monoamine oxidase inhibition. Advances in biochem. Psychopharmacol. 5, 441–444 (1972).
Partridge, S. M.: The part played by oxidation in the synthesis and breakdown of connective tissue. J. Soc. Leather Trades Chemistry 49, 41–52 (1965).
Partridge, S. M., Elsden, D. F., Thomas, J.: Constitution of the cross-linkages in elastin. Nature (Lond.) 197, 1297–1298 (1963).
Partridge, S. M., Elsden, D. F., Thomas, J., Dorfman, A., Telser, A., Ho, P.-L.: Biosynthesis of the desmosine and isodesmosine cross-bridges in elastin. Biochem. J. 93, 30–33C (1964).
Partridge, S. M., Elsden, D. F., Thomas, J., Dorfman, A., Telser, A., Ho, P.-L.: Incorporation of labelled lysine into the desmosine cross-bridges in elastin. Nature (Lond.) 209, 399–400 (1965).
Pau, R. N., Acheson, R. M.: The identification of 3-hydroxy-4-O-β-D-glucosidobenzyl alcohol in the left colleterial gland of Blaberus discoidalis. Biochim. biophys. Acta (Amst.) 158, 206–211 (1968).
Pedersen, P. L., Schnaitman, C. A.: The oligomycin-sensitive adenosine diphosphate-adenosine triphosphate exchange in an inner membrane matrix fraction of rat liver mitochondria. J. biol. Chem. 244, 5065–5073 (1969).
Pegg, A. E., Williams-Ashman, H. G.: Biosynthesis of putrescine in the prostate gland of the rat. Biochem. J. 108, 533–539 (1968a).
Pegg, A. E., Williams-Ashman, H. G.: Stimulation of decarboxylation of S-adenosylmethionine by putrescine in mammalian tissues. Biochem. biophys. Res. Commun. 30, 76–82 (1968b).
Piez, K. A.: Cross-linking of collagen and elastin. Ann. Rev. Biochem. 37, 547–570 (1968).
Piez, K. A., Miller, E. J., Lane, J. M., Butler, W. T.: Localization of chemical and structural features on the collagen molecule. In: Chemistry and Molecular Biology of the Intercellular Matrix (Balazs, E. A., Ed.), Vol. I, p. 117–125. London-New York: Academic Press 1970.
Pinnell, S. R., Martin, G. R.: The cross-linking of collagen and elastin in enzymatic conversion of lysine in peptide linkage to α-aminoadipic-δ-semialdehyde (allysine) by an extract from bone. Proc. nat. Acad. Sci. (Wash.) 61, 708–716 (1968).
Pugh, C. E. M., Quastel, J. H.: Oxidation of aliphatic amines by brain and other tissues. Biochem. J. 31, 286–291 (1937a).
Pugh, C. E. M., Quastel, J. H.: Oxidation of amines by animal tissues. Biochem. J. 31, 2306–2321 (1937b).
Racker, E., Proctor, H.: Reconstitution of the outer mitochondrial membrane with mono-amine oxidase. Biochem. biophys. Res. Commun. 39, 1120–1125 (1970).
Ragland, J. B.: Multiplicity of mitochondrial monoamine oxidases. Biochem. biophys. Res. Commun. 31, 203–208 (1968).
Raina, A.: Studies on the determination of spermidine and spermine and their metabolism in the developing chick embryo. Acta physiol. scand. 60, suppl. 218, 1–81 (1963).
Randall, L. O.: Oxidation of phenethylamine derivatives by amine oxidase. J. Pharmacol. exp. Ther. 88, 216–220 (1946).
Rauch, N., Rauch, R. J.: Isoenzymes of amine oxidase in human plasma and other tissues. Experientia (Basel) 29, 215–217 (1973).
Rauterberg, J., Fietzek, P., Rexrodt, F., Becker, V., Stark, N., Kühn, K.: The amino acid sequence of the carboxyterminal nonhelical cross link region of the α1 chain of calf skin collagen. FEBS Letters 21, 75–79 (1972).
Richter, D.: Adrenaline and amine oxidase. Biochem. J. 31, 2022–2028 (1937).
Riley, W. D., Snell, E. E.: Histidine decarboxylase of Lactobacillus 30a. V. Origin of enzyme-bound pyruvate separation of non-identical subunits. Biochemistry 9, 1485–1491 (1970).
Robertson, J. D.: Cell membranes and the origin of mitochondria. In: Regional Neurochemistry (Kety, S. S., Elkes, J.), p. 497–534. Oxford-London-New York-Paris: Pergamon Press 1961.
Robinson, R. G., Gershon, M. D.: Synthesis and uptake of 5-hydroxytryptamine by the myenteric plexus of the guinea pig ileum: a histochemical study. J. Pharmacol. exp. Ther. 178, 311–324 (1971).
Roensch, L. F., Savage, J. E., O'Dell, B. L.: Purification and characterization of tropoelastin from copper deficient chick aorta. Fed. Proc. 31, 480 Abst. (1972).
Rojkind, M., Hamabata, A., González, E., Rendon, G.: Intermolecular cross-links in rat skin and rat tail collagen. In: Chemistry and Molecular Biology of the Intercellular Matrix (Balazs, E. A., Ed.), Vol. I, p. 293–303. London and New York: Academic Press 1970.
Ross, L. L., Gershon, M. D.: Electron microscopic radioautographic and fluorescence localization of sites of 5-hydroxytryptamine (5-HT) uptake in the myenteric plexus of the guinea-pig ileum. J. Cell Biol. 55, 220a (1972).
Rucker, R. B., O'Dell, B. L.: Connective tissue amine oxidase. I. Purification of bovine aorta amine oxidase and its comparison with plasma amine oxidase. Biochim. biophys. Acta (Amst.) 235, 32–43 (1971).
Sampath, S. S., Clarke, D. E.: A specific increase in intraneuronal monoamine oxidase activity in the rat vas deferens following adrenalectomy. Life Sci. 11 (Part I), 1037, 1–104 (1972).
Sandberg, L. B., Hackett, T. N., Carnes, W. H.: The solubilization of an elastin-like protein from copper-deficient porcine aorta. Biochim. biophys. Acta (Amst.) 181, 201–207 (1969).
Sandberg, L. B., Zeikus, R. D., Coltrain, I. M.: Tropoelastin purification from copper-deficient swine: a simplified method. Biochim. biophys. Acta (Amst.) 236, 542–545 (1971).
Sandler, M.: Catecholamine synthesis and metabolism in man: clinical implications (with special reference to Parkinsonism). In: Handbook of Experimental Pharmacology, Vol. 33 (Blaschko, H., Muscholl, E., Eds.), p. 845–899. Berlin-Heidelberg-New York: Springer 1972.
Sandler, M., Youdim, M. B. H.: Multiple forms of monoamine oxidase: functional significance. Pharmacol. Rev. 24, 331–348 (1972).
Schayer, R. W.: Catabolism of physiological quantities of histamine in vivo. Physiol. Rev. 39, 116–126 (1959).
Schmiedeberg, O.: Über das Verhaltnis des Ammoniaks und der primaren Monoaminbasen zur Harnstoffbildung im Thierkörper. Naunyn-Schmiedebergs Arch. Pharmak. exp. Path. 8, 1–14 (1877).
Schmutzler, W., Hahn, F., Goldschmidt, O., Seseke, G.: Untersuchungen über Substanzen mit histaminaseliberierender Wirkung beim Meerschweinchen. Naunyn-Schmiedebergs Arch. Pharmak. exp. Path. 255, 344–352 (1966a).
Schmutzler, W., Hahn, F., Seseke, G., Bernauer, W.: Über die Herkunft der Plasmahistaminase im anaphylaktischen Schock des Meerschweinchens. Naunyn-Schmiedebergs Arch. Pharmak., exp. Path. 252, 332–338 (1966b).
Schmutzler, W., Knop, J.: Untersuchungen zur Substrat-und Inhibitor-Spezifität der freisetzbaren Leberhistaminase. Biochem. Pharmacol. 17, 1141–1150 (1968).
Schnattman, C., Erwin, V. G., Greenawalt, J. W.: The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J. Cell Biol. 32, 719–735 (1967).
Schnattman, C., Greenawalt, J. W.: Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J. Cell Biol. 38, 158–175 (1968).
Schulz, H.: Histochemische Untersuchungen an den Pansenzotten eines Hausyaks, Bos mutus f. grunniens L. Zool. Anz. 170, 306–310 (1963).
Seligman, A. M., Ueno, H., Morizono, Y., Wasserkrug, H. L., Katzoff, L., Hanker, J. S.: Electron microscopic demonstration of dehydrogenase activity with a new osmiophilic ditetrazolium salt (TC-NBT). J. Histochem. Cytochem. 15, 1–13 (1967).
Shambough, C. F.: Bull. ent. Soc. Amer. 15, 210 (1969). Quoted after Whitehead, 1970.
Sharma, N. N., Bourne, G. H.: Histochemical studies on the distribution of monoamine oxidase, simple esterase and glucose-6-phosphatase in Balantidium coli from chimpanzees. Acta histochem. (Jena) 17, 293–301 (1964).
Sharman, D. F.: The catabolism of catecholamines. Brit. med. Bull. 29, 110–115 (1973).
Shaskan, E. G., Snyder, S. H.: Kinetics of serotonin accumulation into slices from rat brain: relationship to catecholamine uptake. J. Pharmacol. exp. Ther. 175, 404–418 (1970).
Shields, G. S., Coulson, W. F., Kimbell, D. A., Carnes, W. H., Cartwright, G. E., Wintrobe, M. W.: Studies in copper metabolism. XXXII. Cardiovascular lesions in copper-deficient swine. Amer. J. Path. 41, 603–618 (1962).
Shih, J.-H. C., Eiduson, S.: Multiple forms of monoamine oxidase in developing brain: tissue and substrate specificities. J. Neurochem. 18, 1221–1228 (1971).
Shih, J. C., Eiduson, S.: Monoamine oxidase (EC. 1.4.3.4): isolation and characterization of multiple forms of the brain enzyme. J. Neurochem. 21, 41–49 (1973).
Silberstein, S. D., Shein, H. M., Berv, K. R.: Catechol-O-methyl transferase and monoamine oxidase activity in cultured rodent astrocytoma cells. Brain Res. 41, 245–248 (1972).
Silverman, M., Evans, E. A.: The effects of spermine, spermidine and other polyamines on the growth inhibition of Escherichia coli by atabrine. J. biol. Chem. 154, 521–534 (1944).
Simpson, G. G.: The principles of classification of mammals. Bull. Amer. Mus. Nat. Hist. (N.Y.) 85, 1–350 (1945).
Smith, C. L.: Stability of amphibian monoamine oxidase and the inhibitory action of semicarbazide. Comp. Biochem. Physiol. 1, 305–318 (1960).
Smith, D. W., Brown, D. M., Carnes, W. H.: Preparation and properties of salt-soluble elastin. J. biol. Chem. 247, 2427–2432 (1972).
Smith, D. W., Weissman, N., Carnes, W. H.: Cardiovascular studies on copper deficient swine. XII. Partial purification of a soluble protein resembling elastin. Biochem. biophys. Res. Commun. 31, 309–315 (1968).
Smith, T. A.: Polyamine oxidase in higher plants. Biochem. biophys. Res. Commun. 41, 1452–1456 (1970).
Smith, T. A.: The occurrence, metabolism and functions of amines in plants. Biol. Rev. 46, 201–241 (1971).
Smith, T. E., Weissbach, H., Udenfriend, S.: Studies on the mechanism of action of monoamine oxidase: metabolism of N,N-dimethyltryptamine and N,N-dimethyltryptamine-N-oxide. Biochemistry 1, 139–143 (1962).
Snyder, S. H., Fischer, J., Axelrod, J.: Evidence for the presence of monoamine oxidase in sympathetic nerve endings. Biochem. Pharmacol. 14, 363–365 (1965).
Sottocasa, G. L.: Biochemical properties of inner and outer mitochondrial membranes of liver. Biochem. J. 105, 1P–2P (1967).
Sottocasa, G. L., Kuylenstierna, B., Ernster, L., Bergstrand, A.: Separation and some enzymatic properties of the inner and outer membranes of rat liver mitochondria. In: Methods in Enzymology (Colowick, S. P., Kaplan, N. O., Eds.), Vol. 10, p. 448–463. New York and London: Academic Press 1967.
Sourkes, T. L.: Properties of the monoamine oxidase of rat liver mitochondria. Advances in Pharmacol. 6A, 61–69 (1968).
Southgate, J.: Endometrial monoamine oxidase: the effect of sex steroids. Advances in biochem. Psychopharmacol. 5, 263–269 (1972).
Spinks, A., Burn, J. H.: Thyroid activity and amine oxidase in liver. Brit. J. Pharmacol. 7, 93–98 (1962).
Squires, R. F.: Multiple forms of monoamine oxidase in intact mitochondria as characterized by selective inhibitors and thermal stability: a comparison of eight mammalian species. Advances in biochem. Psychopharmacol. 5, 355–370 (1972).
Starcher, B. C.: The effect of pyridoxine deficiency on aortic elastin biosynthesis. Proc. Soc. exp. Biol. (N.Y.) 132, 379–385 (1969).
Starcher, B. C., Partridge, S. M., Elsden, D. F.: Isolation and partial characterization of a new amino-acid from reduced elastin. Biochemistry 6, 2425–2432 (1967).
Stark, M., Rauterberg, J., Kühn, K.: Evidence for a non-helical region at the carboxyl terminus of the collagen molecule. FEBS Letters 13, 101–104 (1971).
Stesina, L. N., Akopyan, Zh. I., Gorkin, V. Z.: Modification of catalytic properties of amine oxidases. FEBS Letters 16, 349–351 (1971).
Strömblad, B. C. R.: Supersensitivity and amine oxidase activity in denervated salivary glands. Acta physiol. scand. 36, 137–153 (1956).
Strömblad, B. C. R.: Observations on amine oxidase in human salivary glands. J. Physiol. (Lond.) 147, 639–643 (1959).
Sykes, B. C., Partridge, S. M.: Isolation of a soluble elastin from lathyritic chicks. Biochem. J. 130, 1171–1172 (1972).
Tabor, C. W., Kellogg, P. D.: Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens. J. biol. Chem. 245, 5424–5433 (1970).
Tabor, C. W., Tabor, H., Bachrach, U.: Identification of the aminoaldehydes produced by oxidation of spermine and spermidine with purified plasma amine oxidase. J. biol. Chem. 239, 2194–2203 (1964).
Tabor, H., Tabor, C. W.: Spermidine, spermine and related amines. Pharmacol. Rev. 16, 245–300 (1964).
Tanzer, M. L.: Isolation and partial characterization of intermolecule crosslinks from reconstituted collagen fibres. In: Chemistry and Molecular Biology of the Intercellular Matrix (Balazs, E. A., Ed.), Vol. I, p. 287–292. London-New York: Academic Press 1970.
Tanzer, M. L., Housley, T., Beruba, L., Fairweather, R., Franzblau, C., Gallop, P. M.: Structure of two histamine containing crosslinks from collagen. J. biol. Chem. 248, 393–402 (1973).
Tanzer, M. L., Kefalides, N. A.: Collagen crosslinks: Occurrence in basement membrane collagens. Biochem. biophys. Res. Commun. 51, 775–780 (1973).
Taylor, C. E., Taylor, R. S., Rasmussen, C., Knowles, P. F.: A catalytic mechanism for the enzyme benzylamine oxidase of pig plasma. Biochem. J. 130, 713–728 (1972).
Theiss, E., Schärer, K.: Toxicity of L-dopa and a decarboxylase inhibitor in animal experiments. In: Monoamines, noyaux gris centraux et syndrome de Parkinson (J. de Ajuriaguerra, G. Gauthier, Eds.), p. 497–504. Geneva: Georg; Paris: Masson 1971.
Tipton, K. F.: The purification of pig brain mitochondrial monoamine oxidase. Europ. J. Biochem. 4, 103–107 (1968a).
Tipton, K. F.: The prosthetic groups of pig brain mitochondrial monoamine oxidase. Biochim. biophys. Acta (Amst.) 159, 451–459 (1968 b).
Tipton, K. F.: Some properties of monoamine oxidase. Advances in biochem. Psychopharmacol. 5, 11–24 (1972).
Tipton, K. F.: Biochemical aspects of monoamine oxidase. Brit. Med. Bull. 29, 116–119 (1973).
Tipton, K. F.: Monoamine oxidase. In: Handbook of Physiology and Endocrinology (Roy, O. Greep, E. B., Astwood, Eds.). Washington: Amer. Physiol. Soc., sect. 7. In print.
Tjälve, H.: Catechol-and indolamines in some endocrine cell systems. An autoradiographical, histochemical and radioimmunological study. Acta physiol. scand. Suppl. 360, 1–22 (1971).
Tranzer, J. P., Thoenen, H.: Electronmicroscopic localization of 5-hydroxytryptamine (3,4,5-trihydroxy-phenyl-ethylamine), a new ”false“ sympathetic transmitter. Experientia (Basel) 23, 743–745 (1967).
Traub, W., Piez, K. A.: Chemistry and structure of collagen. Advanc. Protein Chem. 25, 243–352 (1971).
Trendelenburg, U.: Thyroid and hyperglycaemia produced by adrenaline and noradrenaline. Brit. J. Pharmacol. 8, 454–460 (1953).
Trendelenburg, U.: Factors influencing the concentration of catecholamines at the receptors. In: Handbook of Experimental Pharmacology, Vol. 33 (Blaschko, H., Muscholl, E., Eds.), p. 726–761. Berlin-Heidelberg-New York: Springer 1972.
Trendelenburg, U., Draskoczy, P. R., Graefe, K. H.: The influence of intraneuronal monoamine oxidase on neuronal net uptake of noradrenaline and on sensitivity to noradrenaline. Advances in biochem. Psychopharmacol. 5, 371–377 (1972).
Udenfriend, S.: Metabolism of 5-hydroxytryptamine. In: 5-Hydroxytryptamine (Lewis, G. P., Ed.), p. 43–49. London-New York-Paris-Los Angeles: Pergamon Press 1958.
Uttenthal, L. O., Hope, D. B.: Neurophysins and posterior pituitary hormones in the suiformes. Proc. roy. Soc. B 182, 73–87 (1972).
Vane, J. R.: The relative activities of some tryptamine analogues on the isolated rat stomach preparation. Brit. J. Pharmacol. 14, 87–98 (1959).
Walker, W. H., Kearney, E. B., Seng, R. L., Singer, T. P.: The covalently-bound flavin of hepatic monoamine oxidase. 2. Identification and properties of cysteinyl riboflavin. Europ. J. Biochem. 24, 328–331 (1971).
Watanabe, K., Smith, R. A., Inamasu, M., Yasunobu, K. T.: Recent investigations on the prosthetic group of beef plasma amine oxidase. Advances in biochem. Psychopharmacol. 5, 107–117 (1972).
Weaver, R. H., Herbst, E. J.: The oxidation of polyamines by Neisseria perflava. J. biol. Chem. 231, 647–655 (1958).
Weissbach, H., Redfield, B. G., Udenfriend, S.: Soluble monoamine oxidase; its properties and actions on serotonin. J. biol. Chem. 229, 953–963 (1957).
Weissman, N., Shields, G. S., Carnes, W. H.: Cardiovascular studies on copper-deficient swine IV. Content and solubility of the aortic elastin, collagen and hexosamine. J. biol. Chem. 238, 3115–3118 (1963).
Werle, E., von Pechmann, E.: Über die Diamin-oxydase der Pflanzen und ihre adaptive Bildung durch Bakterien. Liebigs Ann. Chem. 562, 44–60 (1949).
Werle, E., Trautschold, I., Aures, D.: Reinigung und Charakterisierung der Diamin-Oxydase aus Erbsen Hoppe-Seyl. Z. physiol. Chem. 326, 200–211 (1961).
Whitehead, D. L.: The role of haemocytes in the biosynthesis of protocatechuate in the cockroach collaterial system. Biochem. J. 119, 65–66P (1970).
Wohlrab, F.: Der histochemische Nachweis der Monoaminoxydase mit thiazolyl-substituierten Tetrazoliumsalzen in Gegenwart von Metallionen. Histochemie 2, 163–175 (1961).
Yagi, K., Ozawa, T., Naoi, M.: Mechanism of enzyme action. V. Demonstration of an initial step of enzyme-substrate complex using D-amino-acid oxidase and D-lactate or D-mandelate. Biochim. biophys. Acta (Amst.) 185, 31–38 (1969).
Yamada, H., Adachi, O., Ogata, K.: Amine oxidases of microorganisms. Part II. Purification and crystallization of amine oxidase of Aspergillus niger. Agricult. biol. Chem. (Tokyo) 29, 649–654 (1965a).
Yamada, H., Adachi, O., Ogata, K.: Amine oxidases of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger. Agricult. biol. Chem. (Tokyo) 29, 864–869 (1965b).
Yamada, H., Adachi, O., Ogata, K.: Amine oxidases in microorganisms. Part IV. Further properties of amine oxidase of Aspergillus niger. Agricult. biol. Chem. (Tokyo) 29, 912–917 (1965c).
Yamada, H., Adachi, O., Ogata, K.: Putrescine oxidase, a diamine oxidase requiring flavin adenine dinucleotide. Agricult. biol. Chem. (Tokyo) 29, 1148–1149 (1965d).
Yamada, H., Kumagai, H., Kawasaki, H., Matsui, H., Ogata, K.: Crystallization and properties of diamine oxidase from pig kidney. Biochem. biophys. Res. Commun. 29, 723–727 (1967a).
Yamada, H., KumaGai, H., Uwajima, T., Ogata, K.: Bacterial monoamine oxidases. Part II. Substrate and inhibitor specificities of tyramine oxidase of Sarcina lutea. Agricult. biol. Chem. (Tokyo) 31, 897–901 (1967b).
Yamada, H., Suzuki, H., Ogura, Y.: Amine oxidases from microorganisms: Stoichiometry of the reaction catalyzed by amine oxidase of Aspergillus niger. Advances in biochem. Psychopharmacol. 5, 185–201 (1972).
Yamada, H., Tanaka, A., Ogata, K.: Putrescine oxidase in Micrococcus rubens. Agricult. biol. Chem. (Tokyo) 29, 260–261 (1965e).
Yamada, H., Uwajima, T., Kumagai, H., Watanabe, M., Ogata, K.: Crystalline tyramine oxidase from Sarcina lutea. Biochem. biophys. Res. Commun. 27, 350–355 (1967c).
Yamada, H., Uwajima, T., Kumagai, H., Watanabe, M., Ogata, K.: Bacterial monoamine oxidases. Part I. Purification and crystallization of tyramine oxidase of Sarcina lutea. Agricult. biol. Chem. (Tokyo) 31, 890–896 (1967d).
Yamada, H., Yasunobu, K. T.: Monoamine oxidase. I. Purification, crystallization and properties of plasma monoamine oxidase. J. biol. Chem. 237, 1511–1516 (1962a).
Yamada, H., Yasunobu, K. T.: Monoamine oxidase. II. Copper, one of the prosthetic groups of plasma monoamine oxidase. J. biol. Chem. 237, 3077–3082 (1962b).
Yamasaki, E., Swindell, R., Reed, D. J.: Some aspects of catalysis by the amine oxidase of pea seedlings. Biochemistry 9, 1206–1210 (1970).
Yasunobu, K. T., Igaue, I., Gomes, L. B.: The purification and properties of beef liver mitochondrial monoamine oxidase. Advances in Pharmacol. 6A, 43–59 (1968).
Yasunobu, K. T., Oi, S.: Mechanistic aspects of the bovine hepatic monoamine oxidase reaction. Advances in biochem. Psychopharmacol. 5, 91–105 (1972).
Youdim, M. B. H.: Multiple forms of monoamine oxidase and their properties. Advances in biochem. Psychopharmacol. 5, 67–77 (1972).
Youdim, M. B. H., Sourkes, T. L.: The flavin prosthetic group of purified rat liver mitochondrial monoamine oxidase. Advances in biochem. Psychopharmacol. 5, 45–53 (1972).
Young, J. Z.: The life of the Vertebrates, Second Edition. Oxford: Clarendon Press 1962.
Zeller, E. A.: Über den enzymatischen Abbau von Histamin und Diaminen. Helv. chim. Acta 21, 881–890 (1938).
Zeller, E. A.: Diamine oxidase: specificity and mechanism. Advances in biochem. Psychopharmacol. 5, 167–180 (1972).
Zeller, E. A.: Third International Catecholamine Symposium, Strasbourg 1973. In print.
Zeller, E. A., Barsky, J., Berman, E. R.: Amine oxidases XL Inhibition of monoamine oxidase by 1-isonicotinyl-2-isopropylhydrazine. J. biol. Chem. 214, 267–274 (1955).
Zile, M. H.: Effect of thyroxine and related compounds in monoamine oxidase activity. Endocrinology 66, 311–312 (1960).
Zile, M., Lardy, H. A.: Monoamine oxidase activity in liver of thyroid-fed rats. Arch. Biochem. 82, 411–421 (1959).
Zubrzycki, Z., Staudinger, H. J.: Kinetik, intrazelluläre Lokalisation und Induzierbarkeit der Monoaminoxydase. Hoppe-Seylers Z. physiol. Chem. 348, 639–644 (1967).
These references have been added in proof
Bardsley, W.C., Crabbe, M.J.C., Scott, I.V.: The amine oxidases of hnman placenta and pregnancy plasma. Biochem. J. 139, 169–181 (1974).
Murphy, D.L.: Technical strategies for the study of catecholamines in man. In: Frontiers in Catecholamine Research (Usdin, E., Snyder, S.H., Eds.), p. 1077–1082. New York, Toronto, Oxford, Sydney and Braunschweig: Pergamon Press Inc. 1973.
Shannon, W.A., Wasserkrug, H.L., Seligman, A.M.: The ultrastructural localization of monoamine oxidase (MAO) with tryptamine and a new tetrazolium salt, 2-(2′-benzothiazo-lyl)-5-styryl-3-(4′-phthalhydrazydyl) tetrazolium chloride (BSPT). J. Histochem. Cytochem. 22, 170–182 (1974)
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1974 Springer Verlag
About this chapter
Cite this chapter
Blaschko, H. (1974). The natural history of amine oxidases. In: Reviews of Physiology, Biochemistry and Pharmacology, Volume 70. Reviews of Physiology, Biochemistry and Pharmacology, vol 70. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0034294
Download citation
DOI: https://doi.org/10.1007/BFb0034294
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-06716-0
Online ISBN: 978-3-540-38010-8
eBook Packages: Springer Book Archive