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The Influence of Enzymes on Neurohypophysial Hormones and Similar Peptides

  • Chapter
Neurohypophysial Hormones and Similar Polypeptides

Abstract

Oxidizing, reducing and, particularly, proteolytic enzymes have proved capable of affecting oxytocin, vasopressin and related peptides. Their action has been studied for several reasons. Neurohypophysial hormones can be distinguished from each other and from unrelated biologically active compounds by their different susceptibility to enzymatic inactivation. Specifically acting enzymes are valuable tools in studies of hormone structure and structure-activity relationship. The occurrence, distribution and biological significance of enzymes, which may be involved in the metabolism of the neurohypophysial hormones under normal and pathological conditions, have of course been of particular interest. Enzymes may possibly play a physiological role in the release of the hormones from the sites of their synthesis or storage. Enzymes may influence the hormone levels in the circulation. Certainly, enzymes are involved in the breakdown of the hormones in various tissues. The insight into the role and mode of action of the enzymes involved in hormone metabolism has stimulated the synthesis of hormone analogues resistant to enzymatic attack and of hormone precursors which will release active hormones in enzyme-catalyzed reactions. Moreover, compounds have been studied which will either inhibit or activate the hormone-degrading enzymes and thus, it is hoped, enhance or depress, respectively, the action of the hormones themselves.

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Abbreviations

ACTH:

adrenocorticotropic hormone

CAP:

cystine aminopeptidase

EDTA:

ethylene diamine tetraacetate

GSH:

glutathione

GSSG:

oxide form of glutathione

LAP:

leucine aminopeptidase

β-MSH:

β-melanocyte-stimulating hormone

NADP+ :

nicotinamide adenine dinucleotide phosphate

NADPH:

reduced form of nicotinamide adenine dinucleotide phosphate

PCMB:

p-chloromercuribenzoate

References

  • Acher, R.: Évolution moléculaire dans le domaine des hormones neurohypophysaires. VII Giornate Biochim. latine, p. 209-221 (1963).

    Google Scholar 

  • —, et J. Chauvet: La structure de la vasopressine de boeuf. Biochim. biophys. Acta (Amst.) 12, 487–488 (1953).

    CAS  Google Scholar 

  • —: La structure de la vasopressine de boeuf. Biochim. biophys. Acta (Amst.) 14, 421–429 (1954).

    CAS  Google Scholar 

  • —, M.T. Chauvet, et D. Crepy: Isolement d’une nouvelle hormone neurohypophysaire, l’isotocine, présente chez les poissons osseux. Biochim. biophys. Acta (Amst.) 58, 624–625 (1962).

    CAS  Google Scholar 

  • —, et D. Crepy: Phylogénie des peptides neurohypophysaires: Isolement de la meso-tocine (Ileu8-ocytocine) de la grenouille, intermédiaire entre la Ser4-Ileu8-ocytocine des poissons osseux et l’ocytocine des mammifères. Biochim. biophys. Acta (Amst.) 90, 613–615 (1964).

    CAS  Google Scholar 

  • —,et D. Crepy: Phylogénie des peptides neurohypophysaires: Isolement d’une nouvelle hormone, la glumitocine (Ser4-Gln8-ocytocine) présente chez un poisson cartilagineux, la raie (Raia clavata). Biochim. biophys. Acta (Amst.) 107, 393–396 (1965).

    CAS  Google Scholar 

  • —, et M.-T. Lenci: L’ocytocine et la vasopressine du cheval. Bull. Soc. Chim. biol. (Paris) 40, 2005–2018 (1958).

    CAS  Google Scholar 

  • Acher, R., J. Chauvet, et M.-T. Lenci: Purification et structure de l’ocytocine et de la vasopressine du cheval. Biochim. biophys. Acta (Amst.) 31, 545–548 (1959).

    CAS  Google Scholar 

  • M.-T. Lenci —, et C. Fromageot: Chimie des hormones neurohypophysaires. Ergebn. Physiol. 48, 285–327 (1955).

    Google Scholar 

  • Afonso, J.F., and N.G. Farnham: Studies of a new electrophoretic zone in labor and the puerperium and in newborn infants. Amer. J. Obstet. Gynec. 84, 199–205 (1962).

    PubMed  CAS  Google Scholar 

  • Althabe, O., I.C. Arnt, L.A. Branda, and R. Caldeyro-Barcia: Comparison of the milk-ejecting potencies of oxytocin and deamino-oxytocin in lactating women. J. Endocr. 36, 7–14 (1966).

    PubMed  CAS  Google Scholar 

  • Ames, R.G., and H.B. Van Dyke: Thioglycollate inactivation of posterior pituitary anti-diuretic principle as determined in the rat. Proc. Soc. exp. Biol. (N. Y.) 76, 576–578 (1951).

    CAS  Google Scholar 

  • Anastas’eva, N. V.: Effect of pituitrin, quinine, proserine and phenatine on the activity of blood serum oxytocinase of pregnant female rabbits. Nauchn. Zap. Uzhgorodsk. Gos. Univ. 45, 17–21 (1961). Chem. Abstr. 59, 15811 e (1963).

    CAS  Google Scholar 

  • Aragon, G. T.: An evaluation of plasma pitocinase determination in the toxemias of pregnancy. Amer. J. Obstet. Gynec. 55, 961–966 (1948).

    PubMed  CAS  Google Scholar 

  • Arimura, A., and T. Yamaguchi: Serum protein-vasopressin binding and its influence on the pressor activity of the hormone. Jap. J. Physiol. 14, 90–101 (1964).

    CAS  Google Scholar 

  • Arst, H.E., R.T. Manning, and M. Delp: Serum leucine aminopeptidase activity: Findings in carcinoma of the pancreas, pregnancy, and other disorders. Amer. J. med. Sci. 238, 598–609 (1959).

    PubMed  CAS  Google Scholar 

  • Audrain, L., et H. Clauser: Relation entre l’activité physiologique de rocytocine et l’état des son pont disulfure. Biochim. biophys. Acta (Amst.) 30, 191–192 (1958).

    CAS  Google Scholar 

  • —: Mécanisme de l’inactivation de l’ocytocine par le tissu utérin. Biochim. biophys. Acta (Amst.) 38, 494–501 (1960).

    CAS  Google Scholar 

  • Babuna, C., and E. Yenen: Enzymatic determination of placental function. A rapid method. Amer. J. Obstet. Gynec. 95, 925–934 (1966).

    CAS  Google Scholar 

  • Barnafi, L., R. Rosas, T. Pereda, and H. Croxatto: Effect of vasopressin structural modifications on rat renal excretion of Na, K and water. Amer. J. Physiol. 202, 593–596 (1962).

    PubMed  CAS  Google Scholar 

  • Barnes, A.C., and I.B. Sawyer: Measurements of vasopressinase in maternal and cord blood. Amer. J. Obstet. Gynec. 79, 1053–1057 (1960).

    PubMed  CAS  Google Scholar 

  • Barth, T., V. Pliška, and I. Rychlík: Chymotryptic and tryptic cleavage of oxytocin and vasopressin. Collection Czech. Chem. Commun. 32, 1058–1063 (1967).

    CAS  Google Scholar 

  • Barth, T., V. Pliška, and I. Rychlík —, and F. Šorm: Enzymic inactivation of oxytocin. V. Purification and some properties of enzymes from human retroplacental serum. Collection Czech. Chem. Commun. 32, 2327–2336 (1967).

    Google Scholar 

  • Barttk, M., and E. Michnova: Polarographic determination of oxytocinase and a contribution to the characteristics of aminopeptidases. Vet. Med. (Praha) 11, 645-653 (1966). Chem. Abstr. 66, 43882 (1967).

    Google Scholar 

  • Bartošek, I., V. Pliška, I. Rychlík, and F. Šorm: The inactivation of oxytocin in the liver. The proteolytic splitting. Probl. Evolyutsionnoi i Tekhn. Biokhim., Akad. Nauk Sssr, Inst. Biokhim., 276-286 (1964).

    Google Scholar 

  • —, I. Rychlík, and F. Šorm: The inactivation of oxytocin in tissues. Proc. 2nd Int. Pharmacol. Meeting, Prague 1963, 10, 185–188 (1964).

    Google Scholar 

  • Beckman, L., G. Björling, and C. Christodoulou: Pregnancy enzymes and placental polymorphism. II. Leucine aminopeptidase. Acta genet. (Basel) 16, 122–131 (1966a).

    CAS  Google Scholar 

  • C. Christodoulou —: Multiple molecular forms of leucine aminopeptidase in man. Acta genet. (Basel) 16, 223–230 (1966b).

    CAS  Google Scholar 

  • C. Christodoulou —, and M. Grivea: Variations in serum leucine aminopeptidase in pregnant women and in newborn children. Acta Paediat. Scand. 54, 578–580 (1965).

    PubMed  CAS  Google Scholar 

  • Behal, F. J., R.D. Hamilton, C.B. Kanavage, and E.C. Kelly: Studies on aminopeptidases in human blood. Arch. Biochem. 100, 308–312 (1963).

    PubMed  CAS  Google Scholar 

  • Beller, F.K., u. U. Göbelsmann: Der Abbau von natürlichem und synthetischem Oxytocin durch Oxytocinase. Klin. Wschr. 36, 1005–1008 (1958).

    PubMed  CAS  Google Scholar 

  • —: Methodische Probleme der Serumoxytocinase-Bestimmung im Schwangerenserum. Acta endocr. (Kbh.) 31, 467–480 (1959a).

    CAS  Google Scholar 

  • —: Untersuchungen über die Serum-Oxytocinase. Bibl. Gynaec. (Basel) 20, 174–178 (1959b).

    CAS  Google Scholar 

  • —, u. H. Schniz: Quantitative Probleme der Oxytozininaktivierung. Geburtsh. u. Frauen-heilk. 20, 563–569 (1960).

    CAS  Google Scholar 

  • Beránková, Z., I. Rychiík, and F. Šorm: Inhibition of oxytocin inactivation by some pep-tides. Experientia (Basel) 15, 298–299 (1959).

    Google Scholar 

  • Beránková, Z., I. Rychlík, and F. Šorm: Enzymic inactivation of oxytocin. I. Selective inhibitors of oxytocin inactivation. Collection Czech. Chem. Commun. 25, 2575–2580 (1960).

    Google Scholar 

  • F. Šorm —: Enzymic inactivation of oxytocin. II. Fission of some peptide fragments of the oxytocin structure and their derivatives by pregnancy serum and liver cell sap. Collection Czech. Chem. Commun. 26, 1708–1715 (1961).

    Google Scholar 

  • F. Šorm —, and F. Šorm: Enzymic inactivation of oxytocin. III. Desthiooxytocin and S,S’-dibenzyldi-hydrooxytocin as oxytocinase inhibitors and substrates. Collection Czech. Chem. Commun. 26, 2557–2561 (1961).

    Google Scholar 

  • Beránková-Ksandrová, Z., G.W. Bisset, K. JoŠt, I. Krejčé, V. Pliška, J. Rudinger, I. Rychlík, and F. Šorm: Synthetic analogues to oxytocin acting as hormonogens. Brit. J. Pharmacol. 26, 615–632 (1966).

    PubMed  Google Scholar 

  • K. JoŠt, I. Krejčé, V. Pliška, J. Rudinger, I. Rychlík, and F. Šorm —, I. Ryctttík, and F. Šorm: Oxytocin analogues with protracted effects. Proc. 2nd Int. Pharmacol. Meeting, Prague 1963, 10, 181–183 (1964).

    Google Scholar 

  • Birnie, J.H.: The inactivation of posterior pituitary antidiuretic hormone by liver extracts. Endocrinology 52, 33–38 (1953).

    PubMed  CAS  Google Scholar 

  • —, K.E. Blackmore, and H. Heller: Changes in water diuresis and vasopressin inactivation in mice fed on protein deficient diets. Experientia (Basel) 8, 30–31 (1952).

    CAS  Google Scholar 

  • Bisset, G.W.: Effect of tyrosinase preparations on oxytocin, vasopressin and bradykinin. Brit. J. Pharmocol. 18, 405–420 (1962).

    CAS  Google Scholar 

  • —: The effect on milk-ejecting activity of modifying two functional groups in oxytocin. In: Proc. 2nd Int. Pharmacol. Meeting, Prague 1963, 10, 21–30 (1964).

    Google Scholar 

  • Bonow, A., W. Carol, U. S. Wachtel: Die Bestimmung der Serum-Oxytocinase-Aktivität auf chemischem Wege. Zbl. Gynäk. 85, 1537–1542 (1963).

    CAS  Google Scholar 

  • Borov, V. l.: Activity of oxytocinase and cholinesterases at the end of pregancy and during labour. Akusherstwo i Ginekol. 42, 39-42 (1966). Chem. Abstr. 65, 17306f (1966).

    Google Scholar 

  • Braun-Falco, O., u. K. Salfeld: Über das Verhalten der Leucinaminopeptidase-Aktivität im Blutserum und Blaseninhalt. II. Untersuchungen an Patienten mit Psoriasis, Neuroder-matitis diffusa, Dermatitis, Ekzem und anderen Dermatosen. Arch. klin. exp. Derm. 205, 103–111 (1957).

    PubMed  Google Scholar 

  • Bressler, R., and B.R. Forsyth: Serum leucine aminopeptidase activity in normal pregnancy and in patients with hydatidiform mole. New Engl. J. Med. 261, 746–748 (1959).

    PubMed  CAS  Google Scholar 

  • —,and G. Klatskin: Serum leucine aminopeptidase activity in hepatobiliary and pancreatic disease. J. Lab. clin. Med. 56, 417–430 (1960).

    CAS  Google Scholar 

  • Campbell, B.J., B. Thysen, and F.S. Chu: Peptidase catalyzed hydrolysis of antidiuretic hormone in toad bladder. Life Sci. 4, 2129–2140 (1965).

    CAS  Google Scholar 

  • Camu, F., and V. Conard: Effect de l’ocytocine sur l’inactivation de l’insuline par le rein de rat normal in vitro. Arch. int. Pharmacodyn. 162, 247–252 (1966).

    PubMed  CAS  Google Scholar 

  • Carballo, M. A.: Discussion remark. In: Oxytocin. Ed. by R. Caldeyro-Barcia and H. Heller. Proc. Int. Symp., Montevideo 1959, 343 (1961).

    Google Scholar 

  • —, and C. J. Méndez-Bauer: Evolution of oxytocinase during pregnancy and induced labour. Proc. 2nd Uruguayan Congr. Obstet. Ginecol. 2, 300–307 (1957a).

    Google Scholar 

  • —: Placental origin of oxytocinase. Proc. 2nd Uruguayan Congr. Obstet. Ginec. 2, 308–313 (1957b).

    Google Scholar 

  • Centaro, A., P. Periti, and G. De Laurentiis: Oxytocin and oxytocinase activity of the blood and myometrium of women in labor. Riv. Ostet. Ginec. 16, 297–326 (1961).

    PubMed  CAS  Google Scholar 

  • Cespedes, J., and H. Croxatto: Action of oxidants (thiol antagonists) on the oxytocinase activity of blood serum. Bol. Soc. Biol. Santiago 7, 43–46 (1949).

    CAS  Google Scholar 

  • Chauvet, J., M.-T. Chauvet, et R. Acher: Les hormones neurohypophysaires des mammifêres: Isolement et caractérisation de l’ocytocine et de la vasopressine de la balaine (Ba-laenoptera physedus L.) Bull. Soc. Chim. Biol. (Paris) 45, 1369–1378 (1963).

    CAS  Google Scholar 

  • Christlieb, M.: Über den Abbau von Oxytocin und Vasopressin in vitro. Arch. Exp. Pathol. Pharmakol. 194, 44–51 (1940).

    CAS  Google Scholar 

  • Čihař, M., Z. Beránková, I. Rychlík, and F. Šorm: Enzymic inactivation of oxytocin. IV. Characterization of purified preparations of serum oxytocinase. Collection Czech. Chem. Commun. 26, 2632–2642 (1961).

    Google Scholar 

  • Cooper, D.W.: A serum protein present in pregnant women. Nature (Lond.) 200, 892 (1963).

    CAS  Google Scholar 

  • Crewther, W.G., and F.G. Lennox: Preparation of crystals containing protease from Aspergillus oryzae. Nature (Lond.) 165, 680 (1950).

    CAS  Google Scholar 

  • Croxatto, H.: Hypertensinase action. Inactivation of hypertensin and pressor and oxytocic principles of the posterior pituitary in the organism. Rev. Med. Aliment. (Santiago) 5, 259–271 (1942/1943).

    CAS  Google Scholar 

  • —, J. Alliende, and R. Croxatto: Action of aminopolypeptidase of yeast and hypertensinase of kidney extracts on the oxytocic principle of the posterior pituitary. Rev. Med. Aliment. (Santiago) 5, 228–229 (1942/43a).

    Google Scholar 

  • Croxatto, H., J. Alliende, and R. Croxatto: Action of trypsin and chymotrypsin on the oxytocic principle of the posterior pituitary. Rev. Med. Aliment. (Santiago) 5, 230–231 (1942/43b).

    Google Scholar 

  • R. Croxatto —, W. Badia, and R. Croxatto: Effect of fibrinolysin on oxytocin, vasopressin and hyper-tensinogen. Proc. Soc. exp. Biol. (N. Y.) 69, 422–425 (1948).

    CAS  Google Scholar 

  • R. Croxatto —, and J. Cespedes: Action of cytochrome C on the oxytocinase and vasopressinase activity of blood serum. Bol. Soc. Biol. Santiago 7, 54–57 (1950).

    CAS  Google Scholar 

  • R. Croxatto —, and S. Daza: The effect of thiosorbitol on the inactivation of oxytocin and vasopressin by blood plasma. Bol. Soc. Biol. Santiago 8, 96–100 (1951).

    CAS  Google Scholar 

  • R. Croxatto —, R. Croxatto, and J. Alliende: Destruction of oxytocin by the aminopeptidase of beer yeast and by extracts of hypertensive kidneys. Rev. Soc. argent. Biol. 18, 441–453 (1942).

    CAS  Google Scholar 

  • R. Croxatto —, G. Illanes, and H. Salvestrini: Action of chymotrypsin and trypsin on hypertensin and pressor and oxytocic principles of the posterior pituitary. Rev. Med. Aliment. (Santiago) 5, 300–302 (1942/1943).

    Google Scholar 

  • R. Croxatto, G. Illanes —, and M. Reyes: The effect of hypertensin on the inactivation of oxytocin by the serum of pregnant women. Science 108, 658–659 (1948).

    PubMed  CAS  Google Scholar 

  • R. Croxatto —, and M. Rioseco: Action of carboxypeptidase on pepsitensin, vasopressin and oxytocin. Rev. Soc. argent. Biol. 21, 23–29 (1945).

    CAS  Google Scholar 

  • R. Croxatto — C. Donoso, and R. Croxatto: Effect of amino acids on the inactivation of oxytocin by kidney hypertensinase extracts. Bol. Soc. Biol. Santiago 5, 51–53 (1948a).

    CAS  Google Scholar 

  • R. Croxatto —, G. Illanes, H. Salvestrini, and R. Croxatto: Action of aminopolypeptidase and hypertensinase extracts from kidney on the pressor principle of the post-pituitary. Rev. Med. Aliment. (Santiago) 5, 226–228 (1942/1943).

    CAS  Google Scholar 

  • R. Croxatto —, and J. De la Maza: Action of tyrosinase (extracts of Psalliota Campestris) on vasopressin. Bol. Soc. Biol. Santiago 2, 46–48 (1944).

    Google Scholar 

  • —, T. Pereda, and B. Zamorano: Oxytocic substances in blood serum. In: Oxytocin. Proc. Int. Symp., Montevideo 1959, 412-424 (Publ. 1961).

    Google Scholar 

  • R. Croxatto —, and M. Reyes: Effect of cysteine and glutathione on the oxytocinase activity of blood plasma. Bol. Soc. Biol. Santiago 5, 80–82 (1948).

    CAS  Google Scholar 

  • R. Croxatto —, R. Rosas, and L. Barnafi: Effect of vasopressin and oxytocin on excretion of water and electrolytes (Na, Cl, and K) in the albino rat. Acta physiol. lat.-amer. 6, 147–152 (1956).

    PubMed  CAS  Google Scholar 

  • R. Croxatto —, A. Trautmann, and R. Croxatto: Destruction of hypertensin and the pressor and oxytocic principles of the posterior pituitary by extracts of red blood cells and kidney. Rev. Med. Aliment. (Santiago) 5, 305–308 (1943).

    CAS  Google Scholar 

  • R. Croxatto —, C. Vera, and L. Barnafi: Inactivation of antidiuretic hormone by blood serum of the pregnant woman. Proc. Soc. exp. Biol. (N. Y) 83, 784–786 (1953).

    CAS  Google Scholar 

  • Croxatto, R., H. Croxatto, and J. Sorolla: Aminopeptidase character of hypertensinase. Rev. Med. Aliment. (Santiago) 5, 135–136 (1942/1943).

    CAS  Google Scholar 

  • J. Sorolla —, C. Donoso, and H. Croxatto: Effect of amino acids on the inactivation of vasopressin by kidney hypertensinase extracts. Bol. Soc. Biol. (Santiago) 5, 54–56 (1948b).

    CAS  Google Scholar 

  • Dale, H.H., and H.W. Dudley: On the pituitary active principles and histamine. J. Pharmacol, exp. Ther. 18, 27–42 (1921).

    CAS  Google Scholar 

  • Dicker, S.E.: The inactivation of vasopressin and of oxytocin, in vitro. In: Polypeptides which affect smooth muscles and blood vessels, p. 79-82. Ed. by M. Schachter. Proc. Symp., London 1959, (Pub. 1960).

    Google Scholar 

  • —, and M. Ginsburg: Some observations on the antidiuretic activity of rat serum. Brit. J. Pharmacol. 5, 497–504 (1950).

    Google Scholar 

  • —, and A. L. Greenbaum: The degree of inactivation of the antidiuretic activity of vasopressin by the kidneys and the liver of rats. J. Physiol. (Lond.) 126, 116–123 (1954).

    Google Scholar 

  • —: Inactivation of the antidiuretic activity of vasopressin by tissue homogenates. J. Physiol. (Lond.) 132, 199–212 (1956).

    Google Scholar 

  • —: The destruction of the antidiuretic activity of vasopressin by SH active compounds. J. Physiol. (Lond.) 141, 107–116 (1958).

    Google Scholar 

  • —, and C. Tyler: Inactivation of oxytocin and vasopressin by blood plasma of pregnant women. J. Obstet. Gynaec. Brit. Emp. 63, 690–696 (1956).

    Google Scholar 

  • —, and G.A. Whyley: Inactivation of oxytocin by plasma of pregnant women. J. Physiol. (Lond.) 146, 33–34 P (1959a).

    Google Scholar 

  • —: Inactivation of oxytocin by plasma of pregnant women. J. Obstet. Gynaec. Brit. Emp. 66, 605–609 (1959b).

    Google Scholar 

  • — The role of oxytocinase during pregnancy in man and animals. Acta endocr. (Kbh.) 34, (Suppl. 51), 145 (1960).

    Google Scholar 

  • Dieckmann, W. J., G.F. Egenolf, B. Morley, and R.E. Pottinger: The inactivation of the antidiuretic hormone of the posterior pituitary gland by blood from pregnant patients. Amer. J. Obstet. Gynec. 60, 1043–1050 (1950).

    PubMed  CAS  Google Scholar 

  • Dlouhá, H., M. Kraus, J. Křeček, and V. Pliška: Sensitivity of rats to vasopressin in the weaning period. Physiol. bohemoslov. 14, 217–224 (1965).

    PubMed  Google Scholar 

  • Drewntak, K.: Evaluation of a biochemical method of determining the term of delivery. Ginek. pol. 35, 27–32 (1964a).

    Google Scholar 

  • —: Clinical evaluation of the biochemical method of determining the term of delivery. In: Oxytocin and its analogues, p. 55-58. Ed. by R. Klimek and W. Krol. Polish Endocr. Soc, Krakow (1964b).

    Google Scholar 

  • Dudley, H.W.: Some observations on the active principles of the pituitary gland. J. Pharmacol, exp. Ther. 14, 295–312 (1919).

    CAS  Google Scholar 

  • Van Dyke, H.B., B.F. Chow, R.O. Greep, and A. Rothen: The isolation of a protein from the pars neuralis of the ox pituitary with constant oxytocic, pressor and diuresis-inhibiting activities. J. Pharmacol, exp. Ther. 74, 190–209 (1942).

    Google Scholar 

  • Ehrensing, R.H.: Plasma oxytocinase, cystine and leucine naphthylamidases of snake, turtle and chicken. Proc. Soc. exp. Biol. (N. Y.) 117, 370–373 (1964).

    CAS  Google Scholar 

  • El-Kammah, B.M., and H. Tuppy: Unpublished experiments.

    Google Scholar 

  • Elliott, D.F., and W.S. Peart: The amino acid sequence in a hypertensin. Biochem. J. 65, 246–254 (1957).

    PubMed  CAS  Google Scholar 

  • Embrey, M. P.: The action of desamino-oxytocin on the human pregnant uterus. J. Endocr. 31, 185–189 (1965).

    PubMed  CAS  Google Scholar 

  • Eversole, W. J., J.H. Birnie, and R. Gaunt: Inactivation of posterior pituitary antidiuretic hormone by the liver. Endocrinology 45, 378–382 (1949).

    PubMed  CAS  Google Scholar 

  • Fekete, K.: Beiträge zur Physiologie der Gravidität. Endokrinologie 7, 364–369 (1930).

    Google Scholar 

  • —: Gibt es während der Schwangerschaft ein aktives Hypophysen-Hinterlappenhormon im Blute? Endokrinologie 10, 16–23 (1932).

    CAS  Google Scholar 

  • —: Beiträge zur Erklärung des Geburtseintrittes. Endokrinologie 12, 183–192 (1933).

    CAS  Google Scholar 

  • Folk, J.E., and P.W. Cole: Chymotrypsin C. II. Enzymatic specificity toward several poly-peptides. J. biol. Chem. 240, 193–197 (1965).

    CAS  Google Scholar 

  • Fraser, A. M.: The effect of arginase and of tyrosinase on the activity and composition of posterior pituitary extracts. Rev. canad. Biol. 9, 54–61 (1950).

    PubMed  CAS  Google Scholar 

  • Freudenberg, K., E. Weiss U. H. Biller: Notiz über Oxytocin. Z. Physiol. Chem. 233, 172–173 (1935).

    Google Scholar 

  • U. H. Biller —, u. H. Eyer: Über Insulin und Pitutocin. Naturwissenschaften 20, 685 (1932).

    Google Scholar 

  • Fried, R., u. L. Wüst: Über ein Oxytocin-abbauendes Ferment aus Schweineovarien. Naturwissenschaften 41, 238 (1954).

    CAS  Google Scholar 

  • Fuhrmann, K.: Kolorimetrische Bestimmung und histochemischer Nachweis der Aminopep-tidase an Geweben weiblicher Genitalorgane. Zbl. Gynäk. 81, 1105–1123 (1959).

    CAS  Google Scholar 

  • Fylling, P.: Serum and plasma oxytocinase activity during induction of labour. Acta obstet, gynec. scand. 42, 227–239 (1963).

    CAS  Google Scholar 

  • —: Plasma oxytocinase activity, oestriol and pregnanediol excretion and the effect of induction of labour. Acta obstet, gynec. scand. 43, 58–63 (1964 a).

    CAS  Google Scholar 

  • —: Plasma oxytocinase activity following a single injection of pitocin. Acta obstet, gynec. scand. 43, 103–106 (1964b).

    CAS  Google Scholar 

  • —: Serum and plasma leucine aminopeptidase activity during induction of labor. Scand. J. clin. Lab. Invest. 16, 172–176 (1964c).

    PubMed  CAS  Google Scholar 

  • Ginsburg, M., H. Heller, and S.M. A. Zaidi: Re-appraisal of the evidence for the metabolic conversion of vasopressin into a less active derivative. Nature (Lond.) 178,803–804 (1956).

    CAS  Google Scholar 

  • —, and M.W. Smith: The fate of oxytocin in male and female rats. Brit. J. Pharmacol. 14, 327–333 (1959).

    PubMed  CAS  Google Scholar 

  • Di Girolamo, M., D. Rudman, M.F. Malkin, and L.A. Garcia: Inactivation of insulin by adipose tissue. Diabetes 14, 87–92 (1965).

    Google Scholar 

  • Glendening, M.B., M.A. Titus, S.A. Schroeder, G. Mohun, and E.W. Page: The destruction of oxytocin and vasopressin by the aminopeptidases in sera from pregnant women. Amer. J. Obstet. Gynec. 92, 814–820 (1965).

    PubMed  CAS  Google Scholar 

  • Goebelsmann, U., and F.K. Beller: Separation of cystine-aminopeptidase and leucine-aminopeptidase and their determination in pregnant and nonpregnant women. Z. klin. Chem. 3, 49–54 (1965).

    CAS  Google Scholar 

  • Golubow, J., W. Y. Chan, and V. Du Vigneaud: Effect of human pregnancy serum on avian depressor activities of oxytocin and desamino-oxytocin. Proc. Soc. exp. Biol. (N. Y.) 113, 113–115 (1963).

    CAS  Google Scholar 

  • —, and V. Du Vigneaud: Comparison of susceptibility of oxytocin and desamino-oxytocin to inactivation by leucine aminopeptidase and α-chymotrypsin. Proc. Soc. exp. Biol. (N.Y.) 112, 218–219 (1963).

    CAS  Google Scholar 

  • González-Panizza, V.H., Y. Sica-Blanco, and C. Méndez-Bauer: The fate of injected oxytocin in the pregnant woman near term. In: Oxytocin, p. 347-357. Ed. by R. Caldeyro-Barcia and H. Heller. Proc. Int. Symp., Montevideo 1959 (1961).

    Google Scholar 

  • Green, M.N., K.-C. Tsou, R. Bressler, and A.M. Seligman: The colorimetric determination of leucine aminopeptidase activity with L-leucine-ß-naphthylamide hydrochloride. Arch. Biochem. 57, 458–474 (1955).

    PubMed  CAS  Google Scholar 

  • Gulland, J.M., and T.F. Macrae: The action of proteolytic enzymes on the oxytocic principle of the pituitary gland. Nature (Lond.) 131, 470 (1933a).

    CAS  Google Scholar 

  • —: The oxytocic hormone of the posterior lobe of the pituitary gland. III. The action of preparations of plant proteolytic enzymes. Biochem. J. 27, 1237–1247 (1933b).

    PubMed  CAS  Google Scholar 

  • —: The oxytocic hormone of the posterior lobe of the pituitary gland. IV. The action of preparations of animal proteolytic enzymes, and some observations on the nature of the hormone. Biochem. J. 27, 1383–1393 (1933c).

    PubMed  CAS  Google Scholar 

  • Güntelberg, A.V., and M. Ottesen: Preparation of crystals containing the plakalbumin-forming enzyme from Bacillus subtilis. Nature (Lond.) 170, 802 (1952).

    Google Scholar 

  • Haller, E.W., H. Sachs, N. Sperelakis, and L. Share: Release of vasopressin from isolated guinea pig posterior pituitaries. Amer. J. Physiol. 209, 79–83 (1965).

    PubMed  CAS  Google Scholar 

  • Hankiss, J.E., M. Keszthelyi, and P. Demény: Inactivation of vasopressin by heart muscle. Tohoku J. exp. Med. 87, 168–174 (1965).

    PubMed  CAS  Google Scholar 

  • Hanon, F., and M. Brunaud: Determinism of uterine contraction at parturition. C. R. Soc. Biol. (Paris) 141, 163–164 (1947).

    CAS  Google Scholar 

  • Hanson, H., U. H.G. Mannsfeldt: Zur Aktivitätsbestimmung der Serum-Oxytocinase des menschlichen Schwangeren-Serums unter Verwendung chromogener Substrate. In prepn. (1967a). Untersuchungen über die Angreifbarkeit von Serum-Oxytocinase-Substraten durch Gewebs-Enzyme („Gewebs-Oxytocinase“) tierischer Organe. In prepn. (1967b). Über die Humanplacenta als Synthese-Organ der schwangerschaftsspezifischen Serum-Oxytocinase des Menschen. In prepn. (1967 c)

    Google Scholar 

  • Hardy, S.M., and J.M. Ritchie: Determination of serum oxytocinase (l-cystine-aminopepti-dase) activity. Nature (Lond.) 209, 76–77 (1966).

    CAS  Google Scholar 

  • Hashimoto, T.: Studies on l-cystine-aminopeptidase. I. Biochemical aspect. J. Jap. obstet. gynaec. Soc. 8, 87–95 (1961a).

    CAS  Google Scholar 

  • —: Studies on l-cystine-aminopeptidase. II. Clinical observations. J. Jap. obstet, gynaec. Soc. 8,96–104 (1961b)

    Google Scholar 

  • Hawker, R.W.: Inactivation of antidiuretic hormone and oxytocin during pregnancy. Quart. J. exp. Physiol. 41, 301–308 (1956).

    PubMed  CAS  Google Scholar 

  • —: Antidiuretic substance (ADS) in normal pregnancy and pre-eclamptic toxaemia. J. Endocr. 14, 400–410 (1957).

    PubMed  CAS  Google Scholar 

  • —: Oxytocin and an unidentified oxytocic substance in extracts of blood. In: Oxytocin, 425-436. Proc. Int. Symp., Montevideo 1959 (Publ. 1961).

    Google Scholar 

  • —, and P.A. Robertson: Oxytocin and lactation. J. clin. Endocr. 17, 448–451 (1957).

    PubMed  CAS  Google Scholar 

  • —: Are there two oxytocic hormones? Med. J. Aust. 1958 I, 671–672.

    Google Scholar 

  • —, C.F. Walmsley, V. S. Roberts, and P. A. Robertson: Further observations on oxytocin and oxytocic substance. Med. J. Aust. 1959 I, 460–461.

    Google Scholar 

  • Heller, H.: The metabolism and fate of the neurohypophysial principles. In: The neurohypo-physis, p. 77–96. Ed. by H. Heller. London: Butterworths Scientific Publications (1957).

    Google Scholar 

  • —: Inactivation of vasopressin and oxytocin in vivo. In: Polypeptides which affect smooth muscles and blood vessels, p. 59-69. Ed. by M. Schachter. Proc. Symp., London 1959 (Pub. 1960).

    Google Scholar 

  • —, and F. F. Urban: The fate of the antidiuretic principle of postpituitary extracts in vivo and in vitro. J. Physiol. (London) 85, 502–518 (1935).

    CAS  Google Scholar 

  • —, and S.M.A. Zaidi: The metabolism of exogenous and endogenous antidiuretic hormone in the kidney and liver in vivo. Brit. J. Pharmacol. 12, 284–292 (1957).

    PubMed  CAS  Google Scholar 

  • Hess, R.: Arylamidase activity related to angiotensinase. Biochim. biophys. Acta (Amst.) 99, 316–324 (1965).

    CAS  Google Scholar 

  • Hill, R.L., and E.L. Smith: Leucine aminopeptidase. VII. Action on long chain polypeptides and proteins. J. biol. Chem. 228, 577–600 (1957).

    PubMed  CAS  Google Scholar 

  • —: Complete hydrolysis of glucagon by leucine aminopeptidase. Biochim. biophys. Acta (Amst.) 31, 257–258 (1959).

    CAS  Google Scholar 

  • Hilton, J.G., and R.F. Johnson: Changes in blood oxytocinase during parturition. Amer. J. Obstet. Gynec. 78, 479–482 (1959).

    PubMed  CAS  Google Scholar 

  • Hirschfeld, J., and U. Söderberg: Immuno-electrophoretic demonstration of precipitating components in sera from pregnant women. Nature (Lond.) 187, 332–333 (1960).

    CAS  Google Scholar 

  • Hooper, K. C.: The action of inhibitors on enzymes from human placentae. J. Physiol. (London) 148, 283–290 (1959).

    CAS  Google Scholar 

  • —: The preparation of soluble vasopressinase from human placenta. Biochem. J. 74, 297–300 (1960a).

    PubMed  CAS  Google Scholar 

  • Hooper, K. C.: Some properties of enzymes destroying oxytocin and vasopressin. In: Poly-peptides which affect smooth muscles and blood vessels, p. 83-86. Ed. by M. Schachter. Proc. Symp. (London) 1959 (Pub. 1960b).

    Google Scholar 

  • —: The preparation and properties of cystine esterase. Biochem. J. 78, 409–412 (1961a).

    PubMed  CAS  Google Scholar 

  • —: The catabolism of bradykinin, oxytocin, substance P and vasopressin by homogenate of dog hypothalamus. Biochem. J. 81, 44 P (1961b).

    Google Scholar 

  • —: The catabolism of some physiologically active polypeptides by homogenate of dog hypothalamus. Biochem. J. 83, 511–517 (1962a).

    PubMed  CAS  Google Scholar 

  • —: The intracellular distribution of enzymes inactivating oxytocin in the dog hypothalamus. Biochem. J. 85, 8 P (1962b).

    Google Scholar 

  • —: The enzymic inactivation of some physiologically active polypeptides by different parts of the nervous system. Biochem. J. 88, 398–404 (1963a).

    PubMed  CAS  Google Scholar 

  • —: The effect of pregnancy on the distribution of hypothalamic enzymes inactivating oxytocin. Biochem. J. 88, 67 P (1963b).

    Google Scholar 

  • —: The distribution of hypothalamic peptidases in pregnant and non-pregnant dogs. Biochem. J. 90, 584–587 (1964).

    PubMed  CAS  Google Scholar 

  • —: Some observations on the behaviour of hypothalamic enzymes during the time of blastocyst implantation in the rabbit. Biochem. J. 99, 128–132 (1966a).

    PubMed  CAS  Google Scholar 

  • —: The metabolism of oxytocin during lactation in the rabbit. Biochem. J. 100, 823–826 (1966b).

    PubMed  CAS  Google Scholar 

  • — and D.C. Jessup: The distribution of enzymes destroying oxytocin and vasopressin in human placentae. J. Physiol. (Lond.) 146, 539–549 (1959).

    CAS  Google Scholar 

  • Hopsu, V.K., S. Ruponen, and S. Talanti: Leucine aminopeptidase in the placenta of the rat. Acta histochem. (Jena) 12, 305–309 (1961).

    CAS  Google Scholar 

  • Hugtjenin, R.L., and R.A. Boissonnas: Synthèse de la (N-méthyl-Tyr)2-oxytocine. Helv. chim. Acta 44, 213–231 (1961).

    Google Scholar 

  • Ichaliotis, S.D., and Th. C. Lambrinopotjlos: Preeclampsia associated with decrease in serum oxytocinase. Obstet, and Gynec. 24, 659–661 (1964).

    CAS  Google Scholar 

  • —: Serum oxytocinase in twin pregnancy. Obstet, and Gynec. 25, 270–272 (1965).

    CAS  Google Scholar 

  • Itoh, S., and T. Kikuchi: Inactivation of antidiuretic activity of vasopressin by hypothalamic tissue in the presence of pyridoxal. Jap. J. Physiol. 9, 401–405 (1959).

    CAS  Google Scholar 

  • James, N.T.: Histochemical demonstration of oxytocinase in the human placenta. Nature (Lond.) 210, 1276–1277 (1966).

    CAS  Google Scholar 

  • Johnson, M.J.: Isolation and properties of a pure yeast polypeptidase. J. biol. Chem. 137, 575–586 (1941).

    CAS  Google Scholar 

  • Jones, A.M., and W. Schlapp: The action and fate of injected posterior pituitary extracts in the decapitated cat. J. Physiol. (Lond.) 87, 144–157 (1936).

    CAS  Google Scholar 

  • Jošt, K., and J. Rudinger: Amino acids and peptides. XXXIV. Some peptides of S-ben-zylcysteine. Collection Czech. Chem. Commun. 26, 2345–2354 (1961).

    Google Scholar 

  • —, and F. Šorm: Analogues of oxytocin exerting protracted biological effects. Collection Czech. Chem. Commun. 28, 2021–2030 (1963).

    Google Scholar 

  • Kanazawa, T.: Supplementary studies on blood pitocinase. J. Jap. obstet. gynaec. Soc. 1, 42–72 (1954).

    Google Scholar 

  • Karlin, A.: The in vitro release by the toad bladder of an inhibitor of oxytocin. Biochem. biophys. Res. Commun. 11, 44–49 (1963).

    PubMed  CAS  Google Scholar 

  • Kasafirek, E., K. Jost, J. Rudinger, and F. Srm: Amino acids and peptides. LIV. Synthesis of further extended-chain analogues of oxytocin. Collection Czech. Chem. Commun. 30, 2600–2608 (1965).

    CAS  Google Scholar 

  • —, V. Rábek, J. Rudinger, and F. Šorm: Amino acids and peptides. Lxvi. Synthesis of ten extended-chain analogues of lysine vasopressin. Collection Czech. Chem. Commun. 31, 4581–4591 (1966).

    CAS  Google Scholar 

  • Katzen, H. M., and D. Stetten: Hepatic glutathione-insulin transhydrogenase. Diabetes 11, 271–280 (1962).

    PubMed  CAS  Google Scholar 

  • —, F. Tietze, and D. Stetten: Further studies on the properties of hepatic glutathione-insulin transhydrogenase. J. biol. Chem. 238, 1006–1011 (1963).

    PubMed  CAS  Google Scholar 

  • Kazda, S.: Discussion remark. Proc. 2nd Int. Pharmacol. Meeting, Prague 1963,10,150 (1964).

    Google Scholar 

  • Kleiner, H., et M. Van Rymenant: Détermination placentaire de l’ocytocinase sérique dans l’insuffisance et la mort fétale “in utero”. Rev. franç. Étud. clin. biol. 9, 321–323 (1964).

    PubMed  CAS  Google Scholar 

  • Klimek, R.: Discussion remark. Proc. 2nd. Int. Pharmacol. Meeting, Prague 1963,10, 150 to 151 (1964a).

    Google Scholar 

  • —: Pregnancy and delivery in the light of studies on the oxytocin-oxytocinase system. In: Oxytocin and its analogues, p. 27-38. Ed. by R. Klimek and W. Krol, Polish Endocrinol. Soc, Krakow (1964b).

    Google Scholar 

  • —, u. M. Pietrzycka: Biochemische Methode zur Bestimmung der Oxytocinase und ihre klinische Bewertung. Clin. chim. Acta 6, 326–330 (1961).

    PubMed  CAS  Google Scholar 

  • Klimek, R., M. Pietrzycka, and J. Grochowski: The influence of operative trauma on blood levels of oxytocinase. Clin. chim. Acta 7, 398–402 (1962).

    PubMed  CAS  Google Scholar 

  • Kowlessar, O.D., L.J. Haeffner, and E.M. Riley: Localization of serum leucine amino-peptidase, 5-nucleotidase, and nonspecific alkaline phosphatase by starch-gel electropho-resis: Clinical and biochemical significance in disease states. Ann. N. Y. Acad. Sci. 94, 836–843 (1961).

    PubMed  CAS  Google Scholar 

  • Lambrinopoulos, T. C.: Prolonged pregnancy associated with increase in serum oxytocinase. Obstet, and Gynec. 23, 780–782 (1964).

    CAS  Google Scholar 

  • Larson, E.: Tolerance and fate of the pressor principle of posterior pituitary extract in anesthetized animals. J. Pharmacol, exp. Ther. 62, 346–362 (1938).

    CAS  Google Scholar 

  • —: Fate of the injected oxytocic principle of posterior pituitary in anesthetized cats and dogs. J. Pharmacol, exp. Ther. 67, 175–186 (1939).

    CAS  Google Scholar 

  • Lawler, H.C., S.P. Taylor, A.M. Swan, and V. DF Vigneaud: Prensence of glutamine and asparagine in enzymatic hydrolysates of oxytocin and vasopressin. Proc. Soc. exp. Biol. (N.Y.). 87, 550–552 (1954).

    CAS  Google Scholar 

  • —, and V. Du Vigneaud: Enzymatic evidence for intrinsic oxytocic activity of the pressor-antidiuretic hormone. Proc. Soc. exp. Biol. (N. Y.) 84, 114–116 (1953).

    CAS  Google Scholar 

  • Leblová, S., and I. Rychlík: Inhibition of enzymic inactivation of oxytocin by amino acids. Collection Czech. Chem. Commun. 25, 2926–2929 (1960).

    Google Scholar 

  • Lettow, E., u. Ch. Jaeger: Bestimmung der Leucin-Aminopeptidase-Aktivität im Seru trächtiger Hündinnen. Zbl. Vet.-Med. 12, 388–394 (1965).

    CAS  Google Scholar 

  • Lewis, J.: Serum leucine aminopeptidase values in patients with trophoblastic tumors and in normal pregnancy. Amer. J. Obstet. Gynec. 84, 1407–1411 (1962).

    Google Scholar 

  • Linderstrøm-Lang, K., and M. Ottesen: Formation of plakalbumin from ovalbumin. C. R. Lab. Carlsberg, Ser. Chim. 26, 403 (1949).

    Google Scholar 

  • Lineweaver, H., and D. Burk: The determination of enzyme dissociation constants. J. Amer. chem. Soc. 56, 658–666 (1934).

    CAS  Google Scholar 

  • MacLaren, J. A., R.D. Thornes, C.C. Roby, and D.E. Reid: An immunologic characteristic of the serum of normal pregnancy. Amer. J. Obstet. Gynec. 78, 939–946 (1959).

    PubMed  CAS  Google Scholar 

  • Manunta, G.: On the inactivation of oxytocin in the cow. Boll. Soc. ital. Biol. Sper. 36, 281–284 (1960).

    PubMed  CAS  Google Scholar 

  • —, and A. Marongiu: On the inactivation of oxytocin in Bos taurus, Equus caballus, Equus asinus, Ovis aries, Canis familiaris, Sus scrofa, Lepus cuniculus, Cavia cobaya, Mus nor-vegicus albinus, Mus musculus, Gallus gallus and Columbia livia. Boll. Soc. ital. Biol. Sper. 37, 1–2 (1961).

    PubMed  CAS  Google Scholar 

  • Martin, G.J., J.N. Moss, and R.D. Smyth: Vasopressin potentiation and simulation by bromelain. Arch. int. Pharmacodyn. 152, 445–449 (1964).

    PubMed  CAS  Google Scholar 

  • Martin, P.J., and H.O. Schild: Effect of thiols on oxytocin and vasopressin receptors. Nature (Lond.) 196, 382–383 (1962). Pharmacological antagonism between SH compounds and S-S polypeptides. Proc. 2nd Int. Pharmacol. Meeting, Prague 1963, 10, 109-116 (1964).

    CAS  Google Scholar 

  • De la Maza, J., and H. Croxatto: Action of tyrosinase on oxytocin. Bol. Soc. Biol. Santiago 2, 23–26 (1944).

    Google Scholar 

  • McCartney, C.P., F. J. Vallach, and R.E. Pottinger: Further studies on the inactivation of pitressin antidiuretic effect by the blood of pregnant women. Amer. J. Obstet. Gynec. 63, 847–853 (1952).

    PubMed  CAS  Google Scholar 

  • Melander, S.: Plasma oxytocinase activity. A methodological and clinical study with special reference to pregnancy. Acta endocr. (Kbh.) 49, Suppl. 96, 1–94 (1965).

    Google Scholar 

  • Melander, S.E.J.: Oxytocinase activity of plasma of pregnant women. Nature (Lond.) 191, 176–177 (1961).

    CAS  Google Scholar 

  • Méndez-Bauer, C.J.: In: Oxytocin, p. 342. Proc. Int. Symp., Montevideo 1959 (Pub. 1961).

    Google Scholar 

  • —, and M.A. Carballo: Method for the quantitative determination of oxytocin. Proc. 2nd Congr. Urug. Obstet. Gynec. 2, 291–299 (1957).

    Google Scholar 

  • — —,H.M. Cabot, C.E. Negreiros De Paiva, and V.H. Gonzälez-Panizza: Studies on plasma oxytocinase. In: Oxytocin, Proc. Int. Symp., Montevideo 1959,325-335 (Pub. 1961).

    Google Scholar 

  • Mtlani, L.: Effect of pregnant blood serum on the uteromotor activity of the amniotic fluid. Boll. Soc. ital. Biol. Sper. 27, 679–682 (1951).

    Google Scholar 

  • —, and C. Pinetti: Pitocinase. I. Attempts to influence the inactivation of oxytocin by blood serum of the pregnant woman. Boll. Soc. ital. Biol. Sper. 27, 1–4 (1951).

    Google Scholar 

  • Miller, Z.B., E. Naor, L. Milkovtch, and W.M. Schmidt: Serum levels of cystine aminopeptidase, leucine aminopeptidase, and alkaline phosphatase in single and twin pregnancies. Obstet, and Gynec. 24, 707–715 (1964).

    CAS  Google Scholar 

  • Müller-Hartbtjrg, W., H. Nesvadba U. H. Tuppy: Die Anwendung einer chemischen Methode zur Bestimmung des Oxytocinasespiegels im Schwangerenserum. Arch. Gynäk. 191, 442–456 (1959).

    Google Scholar 

  • Munsick, R.A., W.H. Sawyer, and H.B. Van Dyke: Avian neurohypophysial hormones: pharmacological properties and tentative identification. Endocrinology 66, 860–871 (1960).

    CAS  Google Scholar 

  • Nagatsu, I., L. Gillespie, J.M. George, J.E. Folk, and G.G. Glenner: Serum aminopepti-dases, “angiotensinase”, and hypertension. II. Amino acid ß-naphthylamide hydrolysis by normal and hypertensive serum. Biochem. Pharmacol. 14, 853–861 (1965).

    CAS  Google Scholar 

  • Namiki, H. (1952), see Kanazawa (1954).

    Google Scholar 

  • Page, E.W.: The value of plasma pitocinase determinations in obstetrics. Amer. J. Obstet. Gynec. 52, 1014–1022 (1946).

    PubMed  CAS  Google Scholar 

  • —: A blood test for estimating the week of pregnancy. Science 105, 292–293 (1947).

    PubMed  CAS  Google Scholar 

  • —, M.A. Titus, G. Mohun, and M.B. Glendening: The origin and distribution of oxytoci-nase. Amer. J. Obstet. Gynec. 82, 1090–1095 (1961).

    PubMed  CAS  Google Scholar 

  • Periti, P., A. Centaro, and G. De Laurenths: Oxytocinase activity in the uterus of women in labor and in different conditions of pregnancy. Boll. Soc. ital. Biol. Sper. 37, 453–455 (1961a).

    PubMed  CAS  Google Scholar 

  • G. De Laurenths —: Oxytocinase in the blood of women in labor. Boll. Soc. ital. Biol. Sper. 37, 455–457 (1961b).

    PubMed  CAS  Google Scholar 

  • Perks, A.M., M.H.I. Dodd, and J.M. Dodd: A neurohypophyseal principle in the elasmo-branch pituitary. Nature (Lond.) 185, 850–851 (1960).

    CAS  Google Scholar 

  • —, and W.H. Sawyer: A new neurohypophyseal principle in an elasmobranch, Raia ocellata. Nature (Lond.) 205, 154–156 (1965).

    CAS  Google Scholar 

  • Pliška, V., T. Barth, and I. Rychlík: Effect of human serum oxytocinase on the antidiu-retic action of lysine vasopressin and oxytocin in the rat. Experientia (Basel) 23, 196–197 (1967).

    Google Scholar 

  • Preddie, E.C.: Structure of a large polypeptide of bovine posterior pituitary tissue. J. biol. Chem. 240, 4194–4203 (1965).

    PubMed  CAS  Google Scholar 

  • —, and M. Saffran: Isolation of a large polypeptide from bovine posterior pituitary powder. J. biol. Chem. 240, 4189–4193 (1965).

    PubMed  CAS  Google Scholar 

  • Riad, A.M.: Studies on pregnancy serum cystine aminopeptidase activity’ oxytocinase†. J. Obstet. Gynaec. Brit. Emp. 69, 409–416 (1962).

    PubMed  CAS  Google Scholar 

  • —: Changes in pregnancy serum oxytocinase activity during oxytocin infusion and their physiological significance. J. Obstet. Gynaec. Brit. Cwlth 73, 977–982 (1966).

    CAS  Google Scholar 

  • —, and F.J. Scandrett: Distribution of cystine aminopeptidase activity (oxytocinase) in human pregnancy sera. Nature (Lond.) 193, 372–373 (1962).

    CAS  Google Scholar 

  • Riniker, B., u. R. Schwyzer: Die sterische Einheitlichkeit des synthetischen Val5-Hyper-tensin II-Asp1-ß-amids. Helv. chim. Acta 44, 658–667 (1961).

    CAS  Google Scholar 

  • Rittner, Ch.: Über den immunologischen Nachweis von Aminopeptidasen, insbesondere der Oxytocinase (Cystinaminopeptidase). Z. Immun.-Forsch. 131, 422–433 (1966).

    CAS  Google Scholar 

  • Roth, M.: Fluorimetric assay of some peptidases. West European Symp. Clin. Chem. 4, 10–17 (1964). Chem. Abstr. 63, 2054 g (1965).

    CAS  Google Scholar 

  • Royce, P.C., and G. Sayers: Corticotropin releasing activity of a pepsin labile factor in the hypothalamus. Proc. Soc. exp. Biol. (N.Y.) 98, 677–680 (1958).

    CAS  Google Scholar 

  • Rudman, D., M.F. Malkin, S.J. Brown, L.A. Garcia, and L.L. Abell: Inactivation of adrenocorticotropin, α and β-melanocy te-stimulating hormones, vasopressin, and pituitary fraction H by adipose tissue. J. Lipid Res. 5, 38–45 (1964).

    PubMed  CAS  Google Scholar 

  • —, L.A. Garcia, M. D.I. Girolamo, and L.L. Abell: Inactivation of the adipokinetic property of adrenocorticotropin, ßmelanocyte-stimulating hormone, vasopressin and pituitary fraction H by tissues of the rat and rabbit. Endocrinology 75, 867–876 (1964).

    PubMed  CAS  Google Scholar 

  • Rychlík, I.: Inactivation of oxytocin and vasopressin by tissue enzymes: a basis for the design of analogues. Proc. 2nd. Int. Pharmacol. Meeting, Prague 1963, 10, 153–162 (1964).

    Google Scholar 

  • Rydén, G.: Cystine aminopeptidase and oxytocinase activity in pregnancy. A comparative study in human and rat tissues. Acta obstet, gynec. scand. 45, Suppl. 3 (1966).

    Google Scholar 

  • —, and I. Sjöholm: Assay of oxytocin by rat mammary gland in vitro. Brit. J. Pharmacol. 19, 136–141 (1962).

    Google Scholar 

  • Saameli, K.: Quantitative comparison between oxytocin and four related neurohypophysial peptides on the human uterus in situ. Brit. J. Pharmacol. 23, 176–183 (1964).

    PubMed  CAS  Google Scholar 

  • Sachs, H., and Y. Takabatake: Evidence for a precursor in vasopressin biosynthesis. Endocrinology 75, 943–948 (1964).

    PubMed  CAS  Google Scholar 

  • Sasaki, N.: Antidiuretic substance in the bile. IX. The inactivation by a rat liver extract. Yamaguchi Igaku 9, 116–117 (1960).

    CAS  Google Scholar 

  • Sawyer, W. H.: Inactivation of oxytocin by homogenates of uteri and other tissues from normal and pregnant rats. Proc. Soc. exp. Biol. (N. Y.) 87, 463–465 (1954).

    CAS  Google Scholar 

  • Scalabrino, L., and R. Caracristi: Inhibitory action of liver homogenates in vitro toward oxytocin. Arch. Stud. Fisiopat. Ricambio 24, 525–530 (1960).

    CAS  Google Scholar 

  • Scalabrino, L., R. Caracristi, and P. Pebiti: Liver oxytocinase during experimental cirrhosis by carbon tetrachloride in the rabbit. Boll. Soc. ital. Biol. Sper. 37, 450–452 (1961).

    PubMed  CAS  Google Scholar 

  • Schally, A.V., and J.F. Barrett: On the configuration of a lysine-vasopressin dimer. J. Amer. chem. Soc. 87, 2497–2499 (1965).

    CAS  Google Scholar 

  • —, C.Y. Bowers, A. Kuroshima, Y. Ishida, W.H. Carter, and T.W. Redding: Effect of lysine-vasopressin dimers on blood pressure and some endocrine functions. Amer. J. Physiol. 207, 378–384 (1964).

    PubMed  CAS  Google Scholar 

  • —, and R. Guillemin: Some biological and chemical properties of a lysine-vasopressin dimer. J. biol. Chem. 239, 1038–1041 (1964).

    PubMed  CAS  Google Scholar 

  • —, A. J. Kastin, J.F. Barrett, W.H. Carter, C.Y. Bowers, and W.F. White: On vasode-pressor activity in the hypothalamus. Biochem. Pharmacol. 15, 1805–1811 (1966).

    CAS  Google Scholar 

  • Schockaert, J.-A., and J. Lambillon: Sur la présence d’une substance antagoniste de la vasopressine dans le sérum de femmes enceintes. C. R. Soc. Biol. (Paris) 119, 1194–1197 (1935).

    CAS  Google Scholar 

  • —: Observations complémentaires sur la substance antagoniste de la vasopressine dans le sérum de la femme enceinte. C. R. Soc. Biol. (Paris) 122, 478–480 (1936a).

    CAS  Google Scholar 

  • —: Spécificité de la substance inhibant l’action hypertensive de la vasopressine dans le sérum de la femme enceinte. C. R. Soc. Biol. (Paris) 122, 481–484 (1936b).

    CAS  Google Scholar 

  • Schwartz, I.L., and L.M. Livingston: Cellular and molecular aspects of the antidiuretic action of vasopressins and related peptides. Vitam. and Horm. 22, 261–358 (1964).

    CAS  Google Scholar 

  • —, H. Rasmtjssen, M.A. Schoessler, L. Silver, and C.T.O. Fong: Relation of chemical attachment to physiological action of vasopressin. Proc. nat. Acad. Sci. (Wash.) 46, 1288 to 1298 (1960).

    CAS  Google Scholar 

  • Sciarra, J.J., and D.A. Burress: Serum leucine aminopeptidase in twin pregnancy. Proc. Soc. exp. Biol. (N. Y.) 104, 712–713 (1960).

    CAS  Google Scholar 

  • Segura-Cardona, R.: Inhibition of angiotensin, bradykinin and oxytocin by extracts from several organs. Rev. esp. Fisiol. 20, 27–35 (1964).

    PubMed  CAS  Google Scholar 

  • Semm, K.: Die klinische Bedeutung der Oxytocinasebestimmung. Klin. Wschr. 33, 817–818 (1955).

    PubMed  CAS  Google Scholar 

  • —: Der Abbau von synthetischem Oxytocin. Naturwissenschaften 44, 424 (1957).

    CAS  Google Scholar 

  • —: Die Bildungsstätte der Serum-Oxytocinase. Arch. Gynäk. 191, 57–64 (1958a).

    CAS  Google Scholar 

  • —: Oxytocin und Wehen. Fortschr. Geburtsh. Gynäk. 7, 81–88 (1958b).

    CAS  Google Scholar 

  • —: Das Wehenproblem mit besonderer Berücksichtigung des Oxytocin-Oxytocinasehaushaltes. Z. Geburtsh. Gynäk., Suppl. 154, 1–77 (1960).

    CAS  Google Scholar 

  • —: The significance of oxytocinase in pregnancy and labour. In: Oxytocin, p. 336-340. Proc. Int. Symp., Montevideo 1959, (Pub. 1961).

    Google Scholar 

  • —: Der Abbau von Hypophysenhinterlappenhormon durch eine Phytooxytocinase. Naturwissenschaften 49, 59 (1962 a).

    CAS  Google Scholar 

  • —: Der Abbau von Hypophysenhinterlappenhormon durch pflanzliche Enzyme. Arzneimittel-Forsch. 12, 252–260 (1962b).

    CAS  Google Scholar 

  • —: Der Abbau von Oxytocin durch menschliche und pflanzliche Enzyme. Geburtsh. u. Frauenheilk. 22, 980–982 (1962c).

    CAS  Google Scholar 

  • —: Serum-Oxytocinase-Aktivität in der Placenta. Arch. Gynäk. 199, 265–270 (1963).

    CAS  Google Scholar 

  • —: Oxytocin: Abbau durch Enzyme. Gynaecologia (Basel) 159, 61–63 (1965).

    CAS  Google Scholar 

  • —: Anstieg der Serum-Oxytocinase-Aktivität im Blut nach 17-α-Hydroxyprogesteronkapro-nat-oder Allylöstrenol-Zufuhr. Arch. Gynäk. 202, 459–461 (1965).

    CAS  Google Scholar 

  • —: Desamino-Oxytocin, ein von Schwangerenblut nicht inaktivierbares Wehenhormon. Geburtsh. u. Frauenheilk. 27, 36–42 (1967).

    CAS  Google Scholar 

  • —, and J. Bernhard: Zur Diagnostik des placentaren Stoffwechsels durch die Serum-Oxyto-cinase-Bestimmung im mütterlichen Blut. Arch. Gynäk. 199, 271–278 (1963).

    CAS  Google Scholar 

  • —, and E. Waidl: Histochemische Untersuchungen über die Serum-Oxytocinase-Bildung im menschlichen Trophoblasten. Z. Geburtsh. Gynäk. 158, 165–171 (1962).

    CAS  Google Scholar 

  • —, and H.-J. Wiendl: Über Oxytocin inaktivierende Gewebeextrakte. Zbl. Gynäk. 84, 1669–1674 (1962).

    CAS  Google Scholar 

  • Siegel, I.A.: Leucine aminopeptidase in pregnancy. Obstet, and Gynec. 14, 488–490 (1959).

    CAS  Google Scholar 

  • Sjöholm, I.: Enzymatic inactivation of oxytocin. Acta chem. scand. 18, 889–898 (1964).

    Google Scholar 

  • —: Biochemical studies on oxytocin and oxytocinase. Acta pharm. Suecica 4, 81–96 (1967).

    Google Scholar 

  • —, and G. Rydén: Half-life of oxytocin and lysine-vasopressin in blood of rat at different hormonal stages. Acta pharm. Suecica 4, 23–30 (1967).

    Google Scholar 

  • —, and Å. Ryrfeldt: A procedure for determination of radioactive metabolites from tritiated oxytocin in tissues. Acta pharm. Suecica 4, 77–80 (1967).

    Google Scholar 

  • —, and L. Yman: Preparation of highly purified oxytocinase (cystine aminopeptidase) from retroplacental serum. Acta pharm. Suecica 3, 377–388 (1966a). Electrophoretic studies on oxytocinase (cystine aminopeptidase). Relation between electrophoretically found “isozymes”. Acta pharm. Suecica 3, 389-396 (1966b).

    Google Scholar 

  • Sjöholm, L., and L. Yman: Degradation of oxytocin, lysine-vasopressin, angiotensin II and angiotensin-II-amide by oxytocinase (cystine aminopeptidase). Acta pharm. Suecica 4, 65–76 (1967).

    Google Scholar 

  • —, and F. Sandberg: Purification of oxytocinase (cystine aminopeptidase) by ethanol fractionation. Acta pharm. Suecica 2, 261–266 (1965).

    Google Scholar 

  • Smith, E.E., E.P. Pineda, and A.M. Rutenburg: Localization of serum leucine aminopeptidase activity by paper electrophoresis. Proc. Soc. exp. Biol. (N. Y.). 110, 683–687 (1962).

    CAS  Google Scholar 

  • —, and A. M. Rutenburg: Electrophoretic behaviour of an aminopeptidase of human tissues and serum. Nature (Lond.) 197, 800–801 (1963).

    CAS  Google Scholar 

  • Smith, M.W., and H. Sachs: Inactivation of arginine vasopressin by rat-kidney slices. Bio-chem. J. 79, 663–669 (1961).

    CAS  Google Scholar 

  • Smithies, O.: Zone electrophoresis in starch gels and its application to studies of serum proteins. Advanc. Protein Chem. 14, 65–113 (1959).

    CAS  Google Scholar 

  • Spackman, D.H., E.L. Smith, and D.M. Brown: Leucine aminopeptidase. IV. Isolation and properties of the enzyme from swine kidney. J. biol. Chem. 212, 255–269 (1955).

    PubMed  CAS  Google Scholar 

  • Stepankovskaya, G. K.: The role of oxytocic substances and enzymes destroying them in protracted gestations. Akush. i Ginek. 40, 19–23 (1964). Chem. Abstr. 61, 12465b (1964).

    CAS  Google Scholar 

  • Stoklaska, E., u. E. Wintersberger: Zum Mechanismus des Oxytocin-und Vasopressin-Abbaues durch Schwangerenserum. Arch. Exp. Pathol. Pharmakol. 236, 358–364 (1959).

    CAS  Google Scholar 

  • — Beeinflussung der Oxytocinaseaktivität durch Thymusextrakt. Wien. klin. Wschr. 74, 944–946 (1962).

    PubMed  CAS  Google Scholar 

  • —: Über die Oxytocinasehemmstoffe im Thymusextrakt. Wien. klin. Wschr. 75, 16–17 (1963).

    PubMed  CAS  Google Scholar 

  • Suska-Brzezińska, E., and Z. Ewy: Oxytocinase in hen serum. Bull. Acad. pol. Sci., Ser. Sci. Biol. 13, 17–19 (1965).

    Google Scholar 

  • —, M. Golebska, and Z. Ewy: Biological and chemical determinations of tissue oxytocinase in cows. Acta physiol. pol. 16, 151–158 (1965).

    PubMed  Google Scholar 

  • Thorn, N. A.: Some chemical properties of antidiuretic material in the urine of rats. Acta endocr. (Kbh.) 32, 128–133 (1959).

    CAS  Google Scholar 

  • —, and L. Silver: Chemical form of circulating antidiuretic hormone in rats. J. exp. Med. 105, 575–583 (1957).

    PubMed  CAS  Google Scholar 

  • —, and N.B.S. Willumsen: Inhibitory action of calcium on the inactivation of antidiuretic hormone by rat-kidney slices. Acta endocr. (Kbh.) 44, 563–569 (1963).

    CAS  Google Scholar 

  • Thorpe, W. V.: Experiments on the chemical nature of the oxytocic principle of the pituitary gland. Biochem. J. 20, 374–378 (1926).

    PubMed  CAS  Google Scholar 

  • Titus, M.A., D.H. Reynolds, M.B. Glendening, and E.W. Page: Plasma aminopeptidase activity (oxytocinase) in pregnancy and labor. Amer. J. Obstet. Gynec. 80, 1124–1128 (1960).

    PubMed  CAS  Google Scholar 

  • Tuppy, H.: The amino-acid sequence in oxytocin. Biochim. biophys. Acta (Amst.) 11, 449 to 450 (1953).

    CAS  Google Scholar 

  • —: Enzymic inactivation and degradation of oxytocin and vasopressin. In: Polypeptides which affect smooth muscles and blood vessels, p. 49-58. Ed. by M. Schachter. Proc. Symp., London 1959 (Pub. 1960).

    Google Scholar 

  • —: Biochemical studies of oxytocinase. In: Oxytocin, p. 315-324. Proc. Int. Symp., Montevideo 1959 (Pub. 1961).

    Google Scholar 

  • —, u. G. Kreil: Über die beim tryptischen Abbau von Pferde-Cytochrom C entstehenden Peptide. Mh. Chem. 93, 780–794 (1962).

    CAS  Google Scholar 

  • —, u. H. Michl: Über die chemische Struktur des Oxytocins. Mh. Chem. 84, 1011–1020 (1953).

    CAS  Google Scholar 

  • —, u. H. Nesvadba: Über die Aminopeptidaseaktivität des Schwangerenserums und ihre Beziehung zu dessen Vermögen, Oxytocin zu inaktivieren. Mh. Chem. 88, 977–988 (1957).

    CAS  Google Scholar 

  • —, U. Wiesbauer u. E. Wintersberger: Aminosäure-p-nitroanilide als Substrate für Aminopeptidasen und andere proteolytische Fermente. Z. Physiol. Chem. 329, 278–288 (1962).

    CAS  Google Scholar 

  • E. Wintersberger —: Über die Einwirkung von Neuraminidase auf die Serumoxytocinase. Mh. Chem. 94, 321–328 (1963).

    CAS  Google Scholar 

  • —, u. E. Wintersberger: Reinigung und Eigenschaften der Serum-Oxytocinase. Mh. Chem. 91, 1001–1010 (1960).

    CAS  Google Scholar 

  • —: Investigations of pregnancy serum oxytocinase. Proc. 2nd Int. Pharmacol. Meeting, Prague 1963, 10, 143–151 (1964).

    Google Scholar 

  • Du Vigneaud, V., P.S. Fitt, M. Bodanszky, and M. O’connell: Synthesis and somepharma cological properties of a peptide derivative of oxytocin: glycyloxytocin. Proc. Soc. exp. Biol. (N.Y.) 104, 653–656 (1960).

    CAS  Google Scholar 

  • Du Vigneaud, V., H.C. Lawler, and E.A. Popenoe: Enzymatic cleavage of glycinamide from vasopressin and a proposed structure for this pressor antidiuretic hormone of the posterior pituitary. J. Amer. chem. Soc. 75, 4880–4881 (1953).

    Google Scholar 

  • —, C. Kessler, J.M. Swan, C. W. Roberts, and P.G. Katsoyannis: The synthesis of oxyto-cin. J. Amer. chem. Soc. 76, 3115–3121 (1954).

    Google Scholar 

  • —, and S. Trippett: The sequence of amino acids in oxytocin, with a proposal for the structure of oxytocin. J. biol. Chem. 205, 949–957 (1953).

    CAS  Google Scholar 

  • Vorherr, H., U. G. Hüskens: Adiuretinabbau und Aminopeptidaseaktivität in Placenta-extrakten. Klin. Wschr. 41, 926–928 (1963).

    PubMed  CAS  Google Scholar 

  • Werle, E.: Discussion remark. In: Polypeptides which affect smooth muscles and blood vessels, p. 89-90. Ed. by M. Schachter (1960).

    Google Scholar 

  • —, u. G. Effkemann: Über die oxytocinabbauende Fähigkeit des Schwangerenblutes. Arch. Gynäk. 171, 286–290 (1941).

    Google Scholar 

  • —, A. Hevelke U. K. Buthmann: Zur Kenntnis des oxytocinabbauenden Prinzips des Blutes. Biochem. Z. 309, 270–282 (1941).

    Google Scholar 

  • —, u. A. Kalvelage: Über die Vasopressin-inaktivierende Kraft des Blutes von Schwangeren und die Natur des inaktivierenden Prinzips. Biochem. Z. 308, 405–412 (1941).

    Google Scholar 

  • —, u. L. Maier: Über den Abbau von Oxytocin und Vasopressin durch Milchdrüsenextrakte der Kuh. Naturwissenschaften 41, 380 (1954).

    Google Scholar 

  • —, u. K. Semm: Aktivitätsbestimmung der Serum-Oxytocinase als Schwangerschaftsnachweis. Klin. Wschr. 29, 544–545 (1951).

    Google Scholar 

  • —: Methode zur Schwangerschaftsdiagnose mit Bestimmung des Alters der Frucht. Arch. Gynäk. 187, 106–111 (1955).

    Google Scholar 

  • —: Über die Oxytocinase des Schwangerenblutes. Arch. Gynäk. 187, 449–457 (1956).

    Google Scholar 

  • —,u. R. Enzenbach: Über die Oxytocinase des Schwangerenblutes und der Erythrocyten. Arch. Gynäk. 177, 211–217 (1950).

    Google Scholar 

  • Wilken, H.: Die sogenannte „pregnancy zone“, ein neuer Serumfaktor bei Schwangeren. Arch. Gynäk. 199, 243–256 (1963).

    CAS  Google Scholar 

  • Winkhaus, B.: Oxytocinase-Bestimmung bei Kühen unter Berücksichtigung der Bedeutung des Hormons Oxytocin bei der Milchentleerung und Geburtsauslösung. Vet. Med. Diss., München (1954).

    Google Scholar 

  • Wintersberger, E., u. K.P. Chatterjee: Reinigung und Eigenschaften einer Aminopepti-dase der menschlichen Erythrocyten. Mh. Chem. 93, 1268–1278 (1962).

    CAS  Google Scholar 

  • —, W. Müller-Hartburg U. H. Tuppy: Eine einfache Methode zur chemischen Bestimmung der Oxytocinaseaktivität in Schwangerenseren. Clin. chim. Acta 14, 786–792 (1966).

    CAS  Google Scholar 

  • —, E. Stoklaska, H.D. Moed, U. J. Van Dijk: Substituierte Amide des Cystins als Inhibitoren des Oxytocinabbaues durch die Oxytocinase des Schwangerenserums. Rec. Trav. chim. Pays-Bas 83, 1061–1068 (1964).

    Google Scholar 

  • —, u. H. Tuppy: Zonen-Elektrophorese von Aminopeptidasen in Stärkegel. Mh. Chem. 91, 406–411 (1960).

    CAS  Google Scholar 

  • —, u. E. Stoklaska: Über ein kompetitives Substrat der Oxytocinase. Mh. Chem. 91, 577–581 (1960).

    CAS  Google Scholar 

  • Woodbury, R.A., R.P. Ahlquist, B. Abreu, R. Torpin, and W.G. Watson: The inactiva-tion of pitocin and pitressin by human pregnancy blood. J. Pharmacol, exp. Ther. 86, 359–365 (1946).

    CAS  Google Scholar 

  • Yano, F.: Antidiuretic substance in the bile. VI. The stability in some digestive juices and digestive enzymes. Yamaguchi Igaku 9, 107–109 (1960).

    CAS  Google Scholar 

  • Yman, L., and I. Sjöholm: Some physicochemical properties of oxytocinase (cystine amino-peptidase). Acta pharm. Suecica 4, 13–22 (1967).

    CAS  Google Scholar 

  • Zamello, J., and J.M. Zgliczynski: Blood peroxidase activity in women in the perinatal period. Ginek. pol. 36, 147–151 (1965).

    PubMed  CAS  Google Scholar 

  • Zaoral, M., V. Pliška, K. Řežábek, and F. Šorm: Synthesis of two lysine-vasopressin analogues with protracted hormonal activity. Collection Czech. Chem. Commun. 28, 747–749 (1963).

    CAS  Google Scholar 

  • —, and F. Šorm: Preparation and biological activity of some new lysine vasopressin analogues. Proc. 2nd Int. Pharmacol. Meeting, Prague 1963, 10, 167–171 (1964).

    Google Scholar 

  • —: Amino acids and peptides LV. Synthesis of Gly-Cys1-lysine-vasopressin and Gly-Cys1-Tyr(Me)2-lysine vasopressin. Collection Czech. Chem. Commun. 30, 2812–2816 (1965).

    CAS  Google Scholar 

  • Zasztowt, O.: On the behaviour of oxytocinase during pregnancy. Roczn. Akad. Med. Mar-chlewskiego 9, 3–7 (1963).

    CAS  Google Scholar 

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    B. Berde

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Tuppy, H. (1968). The Influence of Enzymes on Neurohypophysial Hormones and Similar Peptides. In: Berde, B. (eds) Neurohypophysial Hormones and Similar Polypeptides. Handbuch der experimentellen Pharmakologie / Handbook of Experimental Pharmacology, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-46127-9_3

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