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Enzymes that Inactivate Vasoactive Peptides

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Concepts in Biochemical Pharmacology

Abstract

This chapter deals with the enzymatic inactivation of two types of vasoactive peptides, plasma kinins and angiotensin II. The metabolic fate of other hormonal or exogenous peptides is not discussed here.

Supported in part by USPHS, NIH Grant HE 08764 and Project THEMIS, Office of Naval Research N00014-68-A-0496.

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References

  • Abdul-Karim, R., Assali, N.S.: Pressor response to angiotonin in pregnant and nonpregnant women. Amer. J. Obstet. Gynec. 82, 246–251 (1961).

    PubMed  CAS  Google Scholar 

  • Abe, K., Watanabe, N., Kumagai, N., Miwa, I., Mouri, K., Seki, T., Oikawa, A., Yoshinaga, K.: Assay of kininase activity in human blood. Tohoku J. exp. Med. 86, 77–83 (1965).

    PubMed  CAS  Google Scholar 

  • Abrams, J.S.: Blood pressure response to the portal infusion of angiotensin II. Surg. Forum 17, 133–134 (1966).

    PubMed  CAS  Google Scholar 

  • Allwood, M.J., Lewis, G.P.: Bradykinin and forearm blood flow. J. Physiol. (Lond.) 170, 571–581 (1964).

    CAS  Google Scholar 

  • Amundsen, E., Nustad, K.: Kinin-forming and destroying activities of saliva. Brit. J. Pharmacol. 23, 440–444 (1964).

    PubMed  CAS  Google Scholar 

  • Amundsen, E., Nustad, K.: Kinin-forming and destroying activities of cell homogenates. J. Physiol. (Lond.) 179, 479–88 (1965).

    CAS  Google Scholar 

  • Amundsen, E., Rugstad, H.E.: Influence of some pathogenic bacteria on kinin formation and destruction. Brit. J. Pharmacol. 25, 67–73 (1965).

    PubMed  CAS  Google Scholar 

  • Arman, C.G. van, Nuss, G.W., Winter, C.A., Flataker, L.: Proteolytic enzymes as mediators of pain. In: Pharmacology of pain, p. 25. Ed. by R.K.S. Lim, D. Armstrong and E.G. Pardo. Oxford: Pergamon Press 1968.

    Google Scholar 

  • Armstrong, D., Stewart, J.W.: Spontaneous plasma kinin formation in human plasma collected during labour. Nature (Lond.) 188, 1193 (1960).

    CAS  Google Scholar 

  • Ascheim, R.S., Hammel, E.C., Mearles, R.J., Lubash, G.D.: Human serum, liver and kidney angiotensinases. Biochem. Med. 1, 288–294 (1967).

    CAS  Google Scholar 

  • Bakhle, Y.S.: Conversion of angiotensin I to angiotensin II by cell-free extracts of dog lung. Nature (Lond.) 220, 919–920 (1968).

    CAS  Google Scholar 

  • Bakhle, Y.S., Reynard, A.M., Vane, J.R.: Metabolism of the angiotensins in isolated perfused tissues. Nature (Lond.) 222, 956–959 (1969).

    CAS  Google Scholar 

  • Berger, M., Langhans, J.: Angiotensinase activity in pregnant and nonpregnant women. Amer. J. Obstet. Gynec. 98, 215–228 (1967).

    PubMed  CAS  Google Scholar 

  • Beuzeville, C.A., Lauson, H.D.: Hepatic clearance of angiotensin from plasma of rats and dogs. Fed. Proc. 24, 524 (1965).

    Google Scholar 

  • Biron, P.: Les angiotensinase du plasma humain. Rev. Canad. Biol. 26, 43–53 (1967).

    PubMed  CAS  Google Scholar 

  • Biron, P.: Pulmonary extraction of bradykinin and eledoisin. Rev. Canad. Biol. 27, 75–76 (1968).

    PubMed  CAS  Google Scholar 

  • Biron, P., Baldus, W.P., Summerskill, W.H.J.: Plasma angiotensinase activity in cirrhosis. Proc. Soc. exp. Biol. (N.Y.) 116, 1074–1077 (1964b).

    CAS  Google Scholar 

  • Biron, P., Campeau, L., David, P.: Fate of angiotensin I and II in the human pulmonary circulation. Amer. J. Cardiol. 24, 544–547 (1969).

    PubMed  CAS  Google Scholar 

  • Biron, P., Landesman, R., Hunt, J.C.: Plasma angiotensinase activity in human hypertension. Nature (Lond.) 204, 1096 (1964a).

    CAS  Google Scholar 

  • Biron, P., Meyer, P.: Hepatic extraction of angiotensin after carbon tetrachloride intoxication. Rev. Canad. Biol. 27, 277–279 (1968).

    PubMed  CAS  Google Scholar 

  • Biron, P., Baldus, W.P., Panisset, J.-C.: Removal of angiotensins from the systemic circulation. Canad. J. Physiol. Pharmacol. 46, 175–178 (1968).

    CAS  Google Scholar 

  • Blaquier, P., Bohr, D.F., Taquini, A.C., Jr., Hoobler, S.W.: Renin and angiotensinase content of the kidney of normal and renal hypertensive rats. Proc. Soc. exp. Biol. (N.Y.) 108, 711–715 (1961).

    CAS  Google Scholar 

  • Boissonnas, R.A., Guttmann, St., Jaquenoud, P.-A.: Synthèse de la L-arginyl-L-prolyl-L-prolyl-glycyl-L-phenylalanyl-L-séryl-L-prolyl-L-phénylalanyl-L-arginine, un nonapetide présentant les proprietés de la bradykinine. Helv. chim. Acta 43, 1349–1358 (1960a).

    CAS  Google Scholar 

  • Boissonnas, R.A., Guttmann, St., Jaquenoud, P.-A.: Synthèse de la L-arginyl-L-prolyl-L-prolyl-glycyl-L-phenylalanyl-L-seryl-L-phenylalanyl-L-arginine. Distinction entre cet octapeptide et la bradykinine. Helv. chim. Acta 43, 1481–1487 (1960b).

    CAS  Google Scholar 

  • Bokisch, V.A., Müller-Eberhard, H.J.: Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase. J. exp. Med. (in press) (1970).

    Google Scholar 

  • Boucher, R., Veyrat, R., Champlatn, J. de, Genest, J.: New procedures for measurement of human plasma angiotensin and renin activity levels. Canad. med. Ass. J. 90, 194–201 (1964).

    PubMed  CAS  Google Scholar 

  • Boyd, G.W., Landon, J., Peart, W.S.: Radioimmunoassay for determining plasma-levels of angiotensin II in man. Lancet 1967II, 1002–1005.

    CAS  Google Scholar 

  • Braun-Menéndez, E., Fasciolo, J.C., Leloir, L.F., Muñoz, J.M.: La substancia hipertensora de la sangre del reñón isquemiado. Rev. Soc. argent. Biol. 15, 420–425 (1939).

    Google Scholar 

  • Braun-Menéndez, E., Fasciolo, J.C., Leloir, L.F., Muñoz, J.M.: The substance causing renal hypertension. J. Physiol. (Lond.) 98, 283–298 (1940).

    Google Scholar 

  • Braun-Menéndez, E., Fasciolo, J.C., Leloir, L.F., Muñoz, J.M., Taquini, A.C.: Renal Hypertension. Springfield/Ill.: Charles C. Thomas 1946.

    Google Scholar 

  • Brunner, H.: Resistenz von verschiedenen Angiotensin-II-Isomeren gegen Inaktivierung durch Plasma oder Nierenhomogenat. Arch. exp. Path. 245, 283–284 (1963).

    Google Scholar 

  • Brunner, H., Regoli, D.: Unterschiedliche Empfindlichkeit verschiedener Angiotensinderivate gegen Abbau durch Plasma oder Nierenhomogenat. Experientia (Basel) 18, 504–505 (1962).

    CAS  Google Scholar 

  • Bumpus, F.M., Smeby, R.R., Page, I.H., Khairallah, P.A.: Distribution and metabolic fate of angiotensin II and various derivatives. Canad. med. Ass. J. 90, 190–193 (1964).

    PubMed  CAS  Google Scholar 

  • Camargo, A.C.M., Graeff, F.G.: Subcellular distribution and properties of the bradykinin inactivation system in rabbit brain homogenates. Biochem. Pharmacol. 18, 548–549 (1969).

    PubMed  CAS  Google Scholar 

  • Centaro, A., Periti, P., Sicuteri, F.: Bradykininogen and bradykininase in blood of women during labour. Settim. med. 51, Suppl. I, 70–76 (1963).

    Google Scholar 

  • Chamberlain, M.J., Browse, N.L., Gibson, D.G., Gleeson, J.A.: Angiotensin and renoportal anastomosis. Brit. med. J. 2, 1507–1508 (1964).

    PubMed  CAS  Google Scholar 

  • Chesley, L.C., Talledo, E., Bohler, C.S., Zuspan, F.P.: Vascular reactivity to antiotensin II and norepinephrine in pregnant and nonpregnant women. Amer. J. Obstet. Gynec. 91, 837–842 (1965).

    PubMed  CAS  Google Scholar 

  • Chiang, T.S., Erdös, E.G., Miwa, I., Tague, L.T., Coalson, J.J.: Isolation from a salivary gland of granules containing renin and kallikrein. Circulat. Res. 23, 507–517 (1968).

    PubMed  CAS  Google Scholar 

  • Cohen, L.A., Gage, J.O., Kokame, G.M., Creech, O., Jr.: Hepatic inactivation of angiotensin. Bull. Tulane med. Fac. 26, 295–298 (1967).

    Google Scholar 

  • Croxatto, H.: La accion hipertensinasica; inactivacion de la hipertensina y de los principios presor y ocitocico de la posthipofisis en el organismo. Rev. Med. Aliment. (Santiago) 5, 259–271 (1943).

    CAS  Google Scholar 

  • Croxatto, H., Cruzatt, H.: Ineffectiveness of carboxypeptidase B in inhibiting the pressor effect of incubated human plasma. Experientia (Basel) 25, 59–60 (1969).

    CAS  Google Scholar 

  • Croxatto, R., Croxatto, H.: Comparative study of hypertensinase and proteinase activity of blood plasma. Proc. Soc. exp. Biol. (N.Y.) 61, 330–333 (1946).

    CAS  Google Scholar 

  • Cushman, D.W., Cheung, H.S.: A simple substrate for assay of dog lung angiotensin converting enzyme. Fed. Proc. 28, 799 (1969).

    Google Scholar 

  • Dahlheim, H., Petschauer, K., Thurau, K.: Anreicherung und Charakterisierung der Erythrocytenangiotensinase. Pflügers Arch. 305, 105–117 (1969).

    PubMed  CAS  Google Scholar 

  • Dengler, H., Reichel, G.: Untersuchungen zur intrazellulären Localisation der Renin-und Hypertensinase-Aktivität. Experientia (Basel) 16, 36–40 (1960).

    CAS  Google Scholar 

  • Deutsch, H.F., Diniz, C.R.: Some proteolytic activities of snake venoms. J. biol. Chem. 216, 17–26 (1955).

    PubMed  CAS  Google Scholar 

  • Dexter, L.: The hypertensinase content of plasma of normal, hypertensive and nephrectomized dogs. Ann. intern. Med. 17, 447–450 (1942).

    CAS  Google Scholar 

  • Dodson, L.F.: The pressor response to hypertensin in pregnant rats. Brit. J. exp. Path. 38, 635–639 (1957).

    PubMed  CAS  Google Scholar 

  • Doyle, A.E., Louis, W.J., Osborn, E.C.: Plasma angiotensinase activity on angiotensin II and analogues. Aust. J. exp. Biol. med. Sci. 45, 41–50 (1967).

    PubMed  CAS  Google Scholar 

  • Doyle, A.E., Louis, W.J., Jerums, G., Osborn, E.C.: Metabolism and blood levels following infusion of a radioactive analog of angiotensin. Amer. J. Physiol. 215, 164–168 (1968).

    PubMed  CAS  Google Scholar 

  • Ebensperger, A., Croxatto, H.: Inactivacion de la hipertensina, de la vasopresina y de la ocitocina por los globulos blancos. Rev. Med. Aliment. (Santiago) 6, 243–246 (1945).

    Google Scholar 

  • Edery, H., Lewis, G.P.: Inhibition of plasma kininase activity at slightly acid pH. Brit. J. Pharmacol. 19, 299–305 (1962).

    PubMed  CAS  Google Scholar 

  • Effkemann, G., Werle, E.: Die körpereigenen uteruswirksamen und kreislaufaktiven Wirkstoffe im Schwangerenorganismus. Arch. Gynäk. 171, 1–27 (1941).

    CAS  Google Scholar 

  • Elliott, D.F., Lewis, G.P.: Methionyl-lysyl-bradykinin, a new kinin from ox blood. Biochem. J. 95, 437–447 (1965).

    PubMed  CAS  Google Scholar 

  • Elliott, D.F., Lewis, G.P., Horton, E.W.: The structure of bradykinin — a plasma kinin from ox blood. Biochem. biophys. Res. Commun. 3, 87–91 (1960).

    CAS  Google Scholar 

  • Enomoto, T., Mineshita, S., Oh-Ishi, S., Shigei, T.: Kininase activity of stem bromelain. Jap. J. Pharmacol. 17, 331–332 (1967).

    PubMed  CAS  Google Scholar 

  • Erdös, E.G.: Enzymes that inactive active polypeptides. Biochem. Pharmacol. 8, 112 (1961).

    Google Scholar 

  • Erdös, E.G.: Enzymes that inactivate polypeptides. In: Metabolic factors controlling duration of drug actions, pp. 159–178. Ed. by B.B. Brodie and E.G. Erdös. Oxford: Pergamon Press 1962.

    Google Scholar 

  • Erdös, E.G.: Hypontensive peptides, bradykinin, kallidin and eledoisin. Advanc. Pharmacol. 4, 1–90 (1966).

    Google Scholar 

  • Erdös, E.G., Cano, G., Yang, H.Y.T.: Hypotensive effect of Lys9-bradykinin in the guinea pig. Biochem. Pharmacol. 16, 1035–1041 (1967c).

    PubMed  Google Scholar 

  • Erdös, E.G., McMennamin, M.A., Wohler, J.R.: Presence of carboxypeptidase B in crude kallikrein (Padutin) preparations. Life Sci. 1, 765–769 (1962).

    Google Scholar 

  • Erdös, E.G., Miwa, I.: Effect of endotoxin shock on the plasma kallikrein-kinin system of the rabbit. Fed. Proc. 27, 92–95 (1968).

    PubMed  Google Scholar 

  • Erdös, E.G., Miwa, I., Graham, W.J.: Studies on the evolution of plasma kinins. Kinins of reptilian and avian blood. Life Sci. 6, 2433–2439 (1967b).

    Google Scholar 

  • Erdös, E.G., Renfrew, A.G., Sloane, E.M., Wohler, J.R.: Enzymatic studies on bradykinin and similar peptides. Ann. N.Y. Acad. Sci. 104, 222–234 (1963b).

    Google Scholar 

  • Erdös, E.G., Seki, T., Yang, H.Y.T., Tague, L.L.: Use of insoluble polymers of enzymes in kinin metabolism. Pharmacol. Res. Commun. 1, 152 (1969).

    Google Scholar 

  • Erdös, E.G., Sloane, E.M.: An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem. Pharmacol. 11, 585–592 (1962).

    PubMed  Google Scholar 

  • Erdös, E.G., Sloane, E.M., Wohler, I.M.: Carboxypeptidase in blood and other fluids. I. Properties, distribution and partial purification of the enzyme. Biochem. Pharmacol. 13, 893–905 (1964).

    Google Scholar 

  • Erdös, E.G., Wohler, I.M., Levine, M.I., Westerman, M.P.: Carboxypeptidase in blood and other fluids. Values in human blood in normal and pathological conditions. Clin. chim. Acta 11, 39–43 (1965).

    Google Scholar 

  • Erdös, E.G., Wohler, J.R.: Inhibitors of the in vivo enzymatic inactivation of bradykinin and kallidin. Life Sci. 2, 270–274 (1963a).

    Google Scholar 

  • Erdös, E.G., Wohler, J.R.: Inhibition in vivo of the enzymatic inactivation of bradykinin and kallidin. Biochem. Pharmacol. 12, 1193–1199 (1963b).

    Google Scholar 

  • Erdös, E.G., Wohler, J.R., Levine, M.I.: Blocking of the in vivo effects of bradykinin and kallidin with carboxypeptidase B. J. Pharmacol. exp. Ther. 142, 327–334 (1963a).

    Google Scholar 

  • Erdös, E.G., Yang, H.Y.T.: Inactivation and potentiation of the effects of bradykinin. In: Hypotensive peptides, pp. 235–250. Ed. by E.G. Erdös, N. Back and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Erdös, E.G., Yang, H.Y.T.: An enzyme in microsomal fraction of kidney that inactivates bradykinin. Life Sci. 6, 569–574 (1967).

    PubMed  Google Scholar 

  • Erdös, E.G., Yang, H.Y.T.: Kininases. In: Bradykinin, kallidin and kallikrein, Handbook of Experimental Pharmacology, p. 289. Ed. by E.G. Erdös. Berlin-Heidelberg-New York: Springer 1970.

    Google Scholar 

  • Erdös, E.G., Yang, H.Y.T., Miwa, I.: Kininases. Hoppe-Seylers Z. physiol. Chem. 349, 928 (1968).

    PubMed  Google Scholar 

  • Erdös, E.G., Yang, H.Y.T., Tague, L.L., Manning, N.: Carboxypeptidase in blood and other fluids. III. The esterase activity of the enzyme. Biochem. Pharmacol. 16, 1287–1297 (1967a).

    PubMed  Google Scholar 

  • Fasciolo, J.C.: Formation and destruction of plasma kinins. Acta physiol. lat.-amer. 14, 170–179 (1964).

    PubMed  CAS  Google Scholar 

  • Fasciolo, J.C., Leloir, L.F., Muñoz, J.M., Braun-Menéndez, E.: La hipertensinasa: Su dosaje y distributión. Rev. Soc. argent. Biol. 16, 643–649 (1940).

    CAS  Google Scholar 

  • Ferreira, S.H.: Bradykinin-potentiating factor. In: Hypotensive peptides, pp. 356–367. Ed. by E.G. Erdös, N. Back and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Ferreira, S.H., Vane, J.R.: The disappearance of bradykinin and eledoisin in the circulation and vascular beds of the cat. Brit. J. Pharmacol. 30, 417–424 (1967a).

    PubMed  CAS  Google Scholar 

  • Ferreira, S.H., Vane, J.R.: The detection and estimation of bradykinin in the circulating blood. Brit. J. Pharmacol. 29, 367–377 (1967b).

    PubMed  CAS  Google Scholar 

  • Folk, J.E., Piez, K.A., Carroll, W.R., Gladner, J.A.: Carboxypeptidase B. IV. Purification and characterization of the porcine enzyme. J. biol. Chem. 235, 2272–2277 (1960).

    PubMed  CAS  Google Scholar 

  • Frey, E.K., Kraut, H., Werle, E.: Kallikrein Padutin. Stuttgart: Ferdinand Enke 1950.

    Google Scholar 

  • Frey, E.K., Kraut, H., Werle, E., Vogel, R., Zickgraf-Rüdel, G., Trautschold, I.: Das Kallikrein-Kinin-System und seine Inhibitoren. Stuttgart: Ferdinand Enke 1968.

    Google Scholar 

  • Garbe, G.: Quantitative Kininogenbestimmung in menschlichem Plasma. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 256, 112–118 (1967).

    CAS  Google Scholar 

  • Glenner, G.G., McMillan, P.J., Folk, J.E.: A mammalian peptidase specific for the hydrolysis of N-terminal and α-L-glutamyl and aspartyl residues. Nature (Lond.) 194, 867 (1962).

    CAS  Google Scholar 

  • Goffinet, J.A., Mulrow, P.J.: Estimation of angiotensin clearance by an in vivo assay. Clin. Res. 11, 408 (1963).

    Google Scholar 

  • Goldacker, I.U. v., Oelkers, W.: Aminopeptidaseaktivität gegen Angiotensin II-Amid im Serum von Gesunden, Schwangeren, Hypertonikern und Leberkranken. Z. klin. Chem. u. klin. Biochem. 7, 250–252 (1969).

    Google Scholar 

  • Gollan, F., Richardson, E., Goldblatt, H.: Studies on plant hypertensinase. J. exp. Med. 87, 29–39 (1948).

    PubMed  CAS  Google Scholar 

  • Greenbaum, L.M., Kim, K.S.: The kinin-forming and kininase activities of rabbit polymorphonuclear leucocytes. Brit. J. Pharmacol. 29, 238–247 (1967).

    PubMed  CAS  Google Scholar 

  • Greenbaum, L.M., Yamafuji, K.: The in vitro inactivation and formation of plasma kinins by spleen cathepsins. Brit. J. Pharmacol. 27, 230–238 (1966).

    PubMed  CAS  Google Scholar 

  • Greene, L.J., Stewart, J.M., Ferreira, S.H.: Bradykinin-potentiating peptides from the venom of Bothrops jararaca. Advanc. exp. Med. Biol. 8, 81–87 (1970).

    CAS  Google Scholar 

  • Haas, E., Goldblatt, H., Lewis, L., Gipson, E.C.: Inhibition of angiotensin and its protection by a cofactor in blood. Amer. J. Physiol. 215, 1420–1428 (1968).

    PubMed  CAS  Google Scholar 

  • Haas, E., Goldblatt, H., Lewis, L., Gipson, E.C.: Angiotensin-protective cofactor. Amer. J. Physiol. 217, 981–987 (1969).

    PubMed  CAS  Google Scholar 

  • Haber, E., Koerner, T., Page, L.B., Kliman, B., Purnode, A.: Application of a radioimmunoassay for angiotensin I to the physiologic measurements of plasma renin activity in normal human subjects. J. clin. Endocr. 29, 1349–1355 (1969).

    PubMed  CAS  Google Scholar 

  • Habermann, E., Blennemann, G.: Über Substrate und Reaktionsprodukte der kininbildenden Enzyme Trypsin, Serum-und Pankreaskallikrein sowie von Crotalusgift. Arch. exp. Pathol. Pharmakol. 249, 357–373 (1964).

    CAS  Google Scholar 

  • Hamberg, U., Rocha e Silva, M.: Studies on the enzymatic inactivation of bradykinin. Acta physiol. scand. 30, 215–225 (1954).

    PubMed  CAS  Google Scholar 

  • Hamberg, U., Rocha e Silva, M.: On the release of bradykinin by trypsin and snake venoms. Arch. int. Pharmacodyn. 110, 222–238 (1957).

    PubMed  CAS  Google Scholar 

  • Harakal, C.D., Collins, D.A.: Plasma hypertensinase in experimental renal hypertension. Circulat. Res. 4, 612–617 (1956).

    PubMed  CAS  Google Scholar 

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

    CAS  Google Scholar 

  • Hickler, R.B., Lauler, D.P., Thorn, G.W.: Plasma angiotensinase activity in patients with hypertension and edema. J. clin. Invest. 42, 635–648 (1963).

    PubMed  CAS  Google Scholar 

  • Hiwada, K.: Studies on plasma angiotensinases in liver disease. Jap. Circulat. J. 32, 1073–1083 (1968).

    CAS  Google Scholar 

  • Hiwada, K., Akutsu, H., Fujimoto, S., Kokubu, T., Yamamura, Y.: Separation of plasma angiotensinases by DEAE Sephadex A-50 column chromatography. Clin. chim. Acta 14, 410–441 (1966).

    PubMed  CAS  Google Scholar 

  • Hodge, R.L., Ng, K.K.F., Vane, J.R.: Disappearance of angiotensin from the circulation of the dog. Nature (Lond.) 215, 138–141 (1967).

    CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Hopsu, V.K., Makinen, K.K., Glenner, G.G.: A peptidase (aminopeptidase B) from cat and guinea pig liver selective for N-terminal arginine and lysine residues. I. Purification and substrate specificity. Acta chem. scand. 20, 1225–1230 (1966a).

    PubMed  CAS  Google Scholar 

  • Hopsu, V.K., Makinen, K.K., Glenner, G.G.: Formation of bradykinin from kallidin-10 by aminopeptidase B. Nature (Lond.) 212, 1271–1272 (1966b).

    Google Scholar 

  • Horton, E.W.: The estimation of urinary kallikrein. J. Physiol. (Lond.) 148, 267–282 (1959).

    CAS  Google Scholar 

  • Itskovitz, H.D., Dudrick, S.J., Dyrda, I., Murphy, J.J.: Plasma angiotensinase activity in hypertensive patients. Arch. intern. Med. 119, 241–246 (1967).

    PubMed  CAS  Google Scholar 

  • Itskovitz, H.D., Miller, L.D.: Renal angiotensinase activity. Circulat. Res. 19, 507–513 (1966).

    PubMed  CAS  Google Scholar 

  • Itskovitz, H.D., Miller, L.D.: Differential studies of angiotensinase activities from several tissue sources. Amer. J. med. Sci. 254, 659–666 (1967).

    PubMed  CAS  Google Scholar 

  • Itskovitz, H.D., Miller, L.D., Ural, W., Zapp, J., White, R.: Inactivation of angiotensin in shock. Amer. J. Physiol. 216, 5–10 (1969).

    PubMed  CAS  Google Scholar 

  • Johnson, D.C., Ryan, J.W.: Degradation of angiotensin II by a carboxypeptidase of rabbit liver. Biochim. biophys. Acta (Amst.) 160, 196–203 (1968).

    CAS  Google Scholar 

  • Kelly, K.A., Nyhus, L.M.: Angiotensin and the liver. Amer. J. Physiol. 210, 305–311 (1966).

    PubMed  CAS  Google Scholar 

  • Kemp, E., Rubin, I.: Removal of angiotensinase from a preparation of renin. Arch. Biochem. Biophys. 96, 56–59 (1962).

    PubMed  CAS  Google Scholar 

  • Khairallah, P.A., Bumpus, F.M., Page, I.H., Smeby, R.R.: Angiotensinase with a high degree of specificity in plasma and red cells. Science 140, 672–674 (1963).

    PubMed  CAS  Google Scholar 

  • Khairallah, P.A., Page, I.H. Plasma angiotensinases. Biochem. Med. 1, 1–8 (1967).

    CAS  Google Scholar 

  • Khairallah, P.A., Page, I.H., Bumpus, F.M., Smeby, R.R.: Angiotensin II: Its metabolic fate. Science 138, 523–525 (1962).

    PubMed  CAS  Google Scholar 

  • Khairallah, P.A., Page, I.H., Bumpus, F.M., Türker, R.K.: Angiotensin tachyphylaxis and its reversal. Circulat. Res. 19, 247–254 (1966).

    PubMed  CAS  Google Scholar 

  • Klaus, D.: Untersuchungen über die Angiotensinase im Serum Gesunder und Kranker. Klin. Wschr. 40, 701–702 (1962).

    PubMed  CAS  Google Scholar 

  • Klaus, D.: Vergleichende Untersuchungen über die Blutdruckwirkung von α-und β-Angiotensin II bei intravenöser Infusion. Klin. Wschr. 44, 1044–1046 (1966).

    PubMed  CAS  Google Scholar 

  • Klaus, D., Daum, A.: Die Wirkung von Aminopeptidase auf den experimentellen renalen Hochdruck der Ratte. Klin. Wschr. 44, 903–904 (1966).

    PubMed  CAS  Google Scholar 

  • Klaus, D., Heizmann, A., Uehleke, H.: Beeinflussung der Blutdruckwirkung von Angiotensin durch Aminopeptidasen und Carboxypeptidase. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 251, 28–38 (1965).

    CAS  Google Scholar 

  • Klaus, D., Kaffarnik, H., Pfeil, H.: Untersuchungen über die Serum-Angiotensinase I, II. Klin. Wschr. 41, 376–385 (1963).

    PubMed  CAS  Google Scholar 

  • Kleine, R., Tille, D.: Charakterisierung der Protamin hydrolysierenden Enzymwirkung des Rattenserums. Acta biol. med. germ. 22, 525–535 (1969).

    PubMed  CAS  Google Scholar 

  • Kokubu, T.: Renal hypertension and angiotensinase. Jap. J. Med. 5, 102–104 (1966).

    CAS  Google Scholar 

  • Kokubu, T., Akutsu, H., Fujimoto, S., Ueda, E., Hiwada, K., Yamamura, Y.: Purification and properties of endopeptidase from rabbit red cells and its process of degradation of angiotensin. Biochim. biophys. Acta (Amst.) 191, 668–676 (1969).

    CAS  Google Scholar 

  • Kokubu, T., Fujimoto, S., Hiwada, K., Akutsu, H., Kato, A., Yamamura, Y.: Inactivation of angiotensin II in liver. Jap. Circulat. J. 31, 879–883 (1967a).

    CAS  Google Scholar 

  • Kokubu, T., Hiwada, K., Ueda, E., Fujimoto, S., Akutsu, H., Kato, A., Yamamura, Y.: Plasma angiotensinase activity in liver disease. Biochem. Med. 1, 54–61 (1967b).

    CAS  Google Scholar 

  • Krivoy, W., Kroger, D.: The preservation of bradykinin by phenothiazines in vitro. Brit. J. Pharmacol. 22, 329–341 (1964).

    PubMed  CAS  Google Scholar 

  • Kroneberg, G., Stoepel, K.: Vergleichende Untersuchungen über die Kreislaufwirkung von Kallikrein (Padutin), Kallidin und Bradykinin. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 245, 284–285 (1963).

    Google Scholar 

  • Kurtz, A.B., Wachsmuth, E.D.: Identification of plasma angiotensinase as aminopeptidase. Nature (Lond.) 221, 92–93 (1969).

    CAS  Google Scholar 

  • Lagrue, G., Meyer, P.: Dosage biologique de l’angiotensinase plasmatique. Technique et premiers résultats. Path. et Biol. 11, 895–897 (1963).

    CAS  Google Scholar 

  • Landesman, R., Biron, P., Castellanos, R., Russa, R.L., Wilson, K.H.: Plasma angiotensinase activity in normal and toxemic pregnancy. Obstet. and Gynec. 22, 316–323 (1963).

    CAS  Google Scholar 

  • Leary, W.P., Ledingham, J.G.: Removal of angiotensin by isolated perfused organs of the rat. Nature (Lond.) 222, 959–960 (1969).

    CAS  Google Scholar 

  • Levin, Y., Pecht, M., Goldstein, L., Katchalski, E.: A water-insoluble polyanionic derivative of trypsin. I. Preparation and properties. Biochemistry 3, 1905–1913 (1964).

    PubMed  CAS  Google Scholar 

  • Loyke, H.F.: Experimental hypertensions treated with CCl4: Measurements of Adrenal Function, Vascular Responsiveness, Angiotensinase and Converting Enzyme. Proc. Soc. exp. Biol. (N.Y.) 115, 1035–1040 (1964).

    CAS  Google Scholar 

  • Lubash, G.D., Bard, R.H., Kline, J.A.: Serum “angiotensinase activity” and female steroidal hormones. Amer. J. med. Sci. 257, 155–163 (1969).

    PubMed  CAS  Google Scholar 

  • Lubash, G.D., Hammel, E.C., Mearles, R.J.: Serum angiotensinase activity in hypertension. Clin. chim. Acta 18, 439–445 (1967).

    CAS  Google Scholar 

  • Lubash, G.D., Hammel, E.C., Mearles, R.J.: Serum angiotensinase activity in cirrhosis. Amer. J. med. Sci. 255, 105–112 (1968).

    PubMed  CAS  Google Scholar 

  • Manca, P., Morandini, G., Mangioni, C., Dimich, D.: L’attività angiotensinasica plasmatica nel corso della gravidanza normale e del puerperio. Minerva ginec. 19, 319–324 (1967).

    PubMed  CAS  Google Scholar 

  • Margolis, J., Bishop, E.A.: Interrelations between different mechanisms of release of biologically active peptides from blood plasma. Nature (Lond.) 194, 749–751 (1962).

    CAS  Google Scholar 

  • Matsunaga, M., Kira, J., Saito, N., Ogino, K., Takayasu, M.: Acid angiotensinase, renin, and acid adenosine triphosphatase in rat kidney lysosomes. Jap. Circulat. J. 32, 137–143 (1968).

    CAS  Google Scholar 

  • Matsunaga, M., Saito, N., Kira, J., Ogino, K., Takayasu, M.: Acid angiotensinase as a lysosomal enzyme. Jap. Circulat. J. 33, 541–551 (1969).

    Google Scholar 

  • McCarthy, D.A., Potter, D.E., Nicolaides, E.D.: An in vivo estimation of the potencies and half-lives of synthetic bradykinin and kallidin. J. Pharmacol. exp. Ther. 148, 117–122 (1965).

    PubMed  CAS  Google Scholar 

  • McDonald, J.K., Zeitman, B.B., Reilly, T.J., Ellis, S.: New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). J. biol. Chem. 244, 2693–2709 (1969).

    PubMed  CAS  Google Scholar 

  • McDonald, J.K., Callahan, P.X., Ellis, S.: Polypeptide degradation by dipeptidyl aminopeptidase I (cathepsin C) and related peptidases. In: Tissue Proteinases: Enzymology and Biology. Ed. by A.J. Barrett, J.T. Dingle, Amsterdam: North-Holland Publishing Co. (in press).

    Google Scholar 

  • Melmon, K.L., Cline, M.J.: Interaction of plasma kinins and granulocytes. Nature (Lond.) 217, 90–92 (1967).

    Google Scholar 

  • Melmon, K.L., Cline, M.J.: The interaction of leukocytes and the kinin system. Biochem. Pharmacol. 17, Suppl., p. 271–281 (1968).

    Google Scholar 

  • Melmon, K.L., Cline, M.J., Hughes, T., Nies, A.S.: Kinins: possible mediators of neonatal circulatory changes in man. J. clin. Invest. 47, 1295–1302 (1968).

    PubMed  CAS  Google Scholar 

  • Methot, A.L., Meyer, P., Biron, P., Lorain, M.P., Lagrue, G., Milliez, P.: Hepatic inactivation of angiotensin. Nature (Lond.) 203, 531–532 (1964).

    CAS  Google Scholar 

  • Mitchell, W.M.: Hydrolysis at arginylproline in polypeptides by clostridiopeptidase B. Science 162, 374–375 (1968).

    PubMed  CAS  Google Scholar 

  • Miwa, I., Erdös, E.G., Seki, T.: Separation of peptide components of urinary kinin (Substance Z). Proc. Soc. exp. Biol. (N.Y.) 131, 768–772 (1969).

    CAS  Google Scholar 

  • Morris, R.E.: In discussion. Canad. med. Ass. J. 90, 194 (1964).

    Google Scholar 

  • Myers, M.G., Robinson, P.R., Morris, R.E.: Relationships of angiotensinase and angiotensin II. Clin. Res. 13, 215 (1965).

    Google Scholar 

  • Nagatsu, I., Gillespie, L., Folk, J.E., Glenner, G.G.: Serum aminopeptidases, “angiotensinase”, and hypertension. I. Degradation of angiotensin II by human serum. Biochem. Pharmacol. 14, 721–728 (1965a).

    PubMed  CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Nagatsu, I., Nagatsu, T., Yamamoto, T., Glenner, G.G., Mehl, J.W.: Purification of aminopeptidase A in human serum and degradation of angiotensin II by the purified enzyme. Biochim. biophys. Acta (Amst.) 198, 255–270 (1970).

    CAS  Google Scholar 

  • Nicolaides, E.D., Dewald, H.A., Craft, M.K.: The synthesis of kinin analogues. Ann. N.Y. Acad. Sci. 104, 15–22 (1963).

    PubMed  CAS  Google Scholar 

  • Nishimura, H., Sokabe, H.: Inhibition of angiotensinases in the rat plasma and kidney. Jap. Heart J. 9, 494–503 (1968).

    PubMed  CAS  Google Scholar 

  • Nugent, F.W., Atendido, W.A., Bulan, M.B., MacDonald, A.J.: Kininase activity in experimental pancreatitis. Nature (Lond.) 211, 207–208 (1966).

    CAS  Google Scholar 

  • Oelkers, W., Goldacker, I.U. v.: Bestimmung der Angiotensinase(Aminopeptidase-)-Aktivität im Serum mit einem DPN-abhängigen optischen Test. Klin. Wschr. 45, 649–653 (1967).

    PubMed  CAS  Google Scholar 

  • Ono, T., Eto, K., Arakawa, K.: Origin of urinary enzymes hydrolysing β-naphthylamides of L-leucine and L-glutamic acid. Clin. chim. Acta 19, 257–265 (1968).

    PubMed  CAS  Google Scholar 

  • Osborn, E.C., Hughes, S.G., Pirie, A.T., Willicombe, P.R., Mahler, R.F.: Clearance studies of angiotensin II and (35S) phenylthiocarbamyl-angiotensin II in the sheep and dog. Cardiovasc. Res. 3, 134–146 (1969).

    CAS  Google Scholar 

  • Osborn, E.C., Jerums, G., Jupp, B.A.: Plasma angiotensinase activity in relation to the breakdown of phenylthiocarbamyl-angiotensin II amide in hypertensive and normotensive patients. Cardiovasc. Res. 2, 31–32 (1968a).

    PubMed  CAS  Google Scholar 

  • Osborn, E.C., Jerums, G., Jupp, B.A.: Blood angiotensinase activity in relation to the breakdown of angiotensin II amide and nonisotopic phenylthiocarbamyl-angiotensin II amide in hypertensive and normotensive patients. Cardiovasc. Res. 2, 33–38 (1968b).

    PubMed  CAS  Google Scholar 

  • Osborne, M.J., d’Auriac, G.A., Meyer, P., Worcel, M.: Mechanism of Extraction of Angiotensin II in coronary and renal circulations. Life Sci. 9, 859–867 (1970).

    CAS  Google Scholar 

  • Page, I.H., Helmer, O.M.: A crystalline pressor substance (angiotonin) resulting from the reaction between renin and renin-activator. J. exp. Med. 71, 29–42 (1940).

    PubMed  CAS  Google Scholar 

  • Page, I.H., Helmer, O.M., Kohlstaedt, K.G., Kempf, G.F., Corcoran, A.C., Taylor, R.D.: A progress report on investigations concerned with the experimental treatment of hypertension with kidney extracts. Ann. intern. Med. 18, 29–42 (1943).

    CAS  Google Scholar 

  • Page, I.H., McCubbin, J.W., editors: Renal Hypertension. Chicago: Year Book Medical Publishers, Inc. 1968.

    Google Scholar 

  • Paskhina, T.S., Trapeznikova, S.S.: Cleavage of depsipeptide analogs of bradykinin by kininase (carboxypeptidase N) from human and rabbit serum. Biokhimiya 32, 527 (1967).

    CAS  Google Scholar 

  • Phelps, P., Prockhop, D.J., McCarty, D.J.: Crystal induced inflammation in canine joints. III. Evidence against bradykinin as a mediator of inflammation. J. Lab. clin. Med. 68, 433–444 (1966).

    PubMed  CAS  Google Scholar 

  • Pickens, P.T., Bumpus, F.M., Lloyd, A.M., Smeby, R.R., Page, I.H.: Measurement of renin activity in human plasma. Circulat. Res. 17, 438–448 (1965).

    PubMed  CAS  Google Scholar 

  • Prado, J.L.: Proteolytic enzymes as kininogenases. In: “Bradykinin, kallidin and kallikrein”, Handbook of Experimental Pharmacology, p. 156. Ed. by E.G. Erdös. Berlin-Heidelberg-New York: Springer 1970.

    Google Scholar 

  • Regoli, D., Riniker, B., Brunner, H.: The enzymatic degradation of various angiotensin II derivatives by serum, plasma or kidney homogenate. Biochem. Pharmacol. 12, 637–646 (1963).

    PubMed  CAS  Google Scholar 

  • Riniker, B.: Recent work on the chemistry and biochemistry of angiotensin II. Metabolism 13, 283–291 (1964).

    Google Scholar 

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

    CAS  Google Scholar 

  • Riniker, B., Schwyzer, R.: Synthetische Analoge des Hypertensins. V. α-L-, β-L-, α-D-und β-D-Asp1-Val5-Hypertensin II; Desamino-Val5-Hypertensin II. Helv. chim. Acta 47, 2357–2374 (1964).

    CAS  Google Scholar 

  • Rocha e Silva, M.: Bradykinin — mechanism of its release by trypsin and kallikrein. Arch. int. Pharmacodyn. 88, 271–282 (1951).

    CAS  Google Scholar 

  • Rocha e Silva, M.: The physiological significance of bradykinin. Ann. N.Y. Acad. Sci. 104, 190–210 (1963).

    Google Scholar 

  • Rocha e Silva, M., Beraldo, W.T., Rosenfeld, G.: Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Amer. J. Physiol. 156, 261–273 (1949).

    PubMed  Google Scholar 

  • Rugstad, H.E.: Kininase production by some microbes. Brit. J. Pharmacol. 28, 315–323 (1966).

    PubMed  CAS  Google Scholar 

  • Rugstad, H.E.: Purification of a kinin-inactivating enzyme from cultures of Pseudomonas aeruginosa. Brit. J. Pharmacol. 30, 134–142 (1967a).

    PubMed  CAS  Google Scholar 

  • Rugstad, H.E.: Characterization of a plasma kinin-inactivating enzyme produced by Pseudomonas aeruginosa. Brit. J. Pharmacol. 30, 425–435 (1967b).

    PubMed  CAS  Google Scholar 

  • Rugstad, H.E.: Degradation of plasma kinins by an enzyme from Pseudomonas aeruginosa. Brit. J. Pharmacol. 31, 401–406 (1967c).

    PubMed  CAS  Google Scholar 

  • Ryan, J.W., Roblero, J., Stewart, J.M.: Inactivation of bradykinin in the pulmonary circulation. Biochem. J. 110, 795–797 (1968a).

    PubMed  CAS  Google Scholar 

  • Ryan, J.W., McKenzie, J.K., Lee, M.R.: A rapid simple method for the assay of renin in rabbit plasma. Biochem. J. 108, 679–685 (1968b).

    PubMed  CAS  Google Scholar 

  • Saameli, K., Eskes, T.K.A.B.: Bradykinin and cardiovascular system: estimation of half-life. Amer. J. Physiol. 203, 261–265 (1962).

    PubMed  CAS  Google Scholar 

  • Saito, N., Sanada, K., Matsunaga, M., Kira, J., Mukaino, S., Ogino, K., Takayasu, M.: Amino acid analysis after degradation of angiotensin II by rat kidney lysosomes. Jap. Circulat. J. 33, 87–93 (1969).

    CAS  Google Scholar 

  • Sambhi, M.P., Barrett, J.D.: Angiotensinase activity in fractionated human plasma and effect of enzyme inhibitors. Clin. Res. 14, 149 (1966).

    Google Scholar 

  • Sambhi, M.P., Barrett, J.D.: Plasma “angiotensinase” activity as a determinant of angiotensin pressor action and tachyphylaxis in the rat. Biochem. Pharmacol. 17, 787–795 (1968).

    PubMed  CAS  Google Scholar 

  • Sapirstein, L.A., Reed, R.K., Page, E.W.: The site of angiotonin destruction. J. exp. Med. 83, 425–439 (1946).

    CAS  Google Scholar 

  • Schachter, M.: Some properties of kallidin, bradykinin and wasp venom kinin. In: Polypeptides which affect smooth muscles and blood vessels, pp. 232–246. Ed. by M. Schachter. Oxford 1960.

    Google Scholar 

  • Schröder, E.: Über Peptidsynthesen. Synthese von Methionyl-Lysyl-Bradykinin, einem Kinin aus Rinderblut. Experientia (Basel) 20, 39 (1964).

    Google Scholar 

  • Schröder, E., Lübke, K.: The Peptides. Vol. II. New York: Academic Press 1966.

    Google Scholar 

  • Schwab, J.: Kininases in leucocytes and other tissues. Nature (Lond.) 195, 345–347 (1962).

    CAS  Google Scholar 

  • Seki, I., Jenssen, T.A., Levin, Y., Erdös, E.G.: Active water-insoluble derivative of renin. Nature (Lond.) 225, 864–865 (1970b).

    CAS  Google Scholar 

  • Seki, I., Yang, H.Y.T., Levin, Y., Jenssen, T.A., Erdös, E.G.: Application of water-insoluble complexes of kininogenases, inhibitors and kininases to kinin research. Advanc. exp. Med. Biol. (in press) (1970a).

    Google Scholar 

  • Shimonaeva, E.E.: Some properties of carboxypeptidase N from rabbit blood serum. Vop. med. Khim 13, 105–107 (1967).

    CAS  Google Scholar 

  • Sicuteri, P., Fanciullacci, M., Del Bianco, P.L., Anselmi, B.: Bradichininasi nel liquido cefalo-rachidiano dell-uomo. Boll. Soc. ital. Biol. sper. 41, 464–466 (1965).

    PubMed  CAS  Google Scholar 

  • Sicuteri, P., Periti, P., Anselmi, B., Fanciullacci, M.: Livelli plasmachininici dell’uomo dopo somministrazione endovenosa ed endoarteria di bradichinina sintetica e naturale. Boll. Soc. ital. Biol. sper. 39, 314–318 (1963).

    PubMed  CAS  Google Scholar 

  • Skeggs, L.T., Lentz, K.E., Kahn, J.R., Dorer, F.E., Levine, M.: Pseudorenin; a new angiotensin-forming enzyme. Circulat. Res. 25, 451–462 (1969).

    PubMed  CAS  Google Scholar 

  • Stewart, J.M.: Synthesis and pharmacology of polistes kinin, a bradykinin homolog. Fed. Proc. 27, 534 (1968).

    Google Scholar 

  • Stewart, J.M., Roblero, J.: Studies on the pulmonary inactivation of bradykinin. In: Symposium on Vasoactive Polypeptides and Inhibitors of Proteolytic Enzymes, pp. 52–55. Tokyo 1967.

    Google Scholar 

  • Suzuki, T., Iwanaga, S.: Snake venoms. In: Bradykinin, kallidin and kallikrein, Handbook of Experimental Pharmacology, p. 193. Ed. by E.G. Erdös. Berlin-Heidelberg-New York: Springer 1970.

    Google Scholar 

  • Suzuki, T., Iwanaga, S., Nagasawa, S., Sato, T.: Purification and properties of bradykininogen and of the bradykinin-releasing and-destroying enzymes in snake venom. In: Hypotensive peptides, pp. 149–160. Ed. by E.G. Erdos, N. Back and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Talledo, O.: Renin-angiotensin system in normal and toxemic pregnancies. II. Inactivation of angiotensin in normal pregnancy. Amer. J. Obstet. Gynec. 97, 571–572 (1967).

    PubMed  CAS  Google Scholar 

  • Teger-Nilsson, A.-C.: Degradation of human fibrinopeptides A and B in blood serum in vitro. Acta chem. scand. 22, 3171–3182 (1968).

    PubMed  CAS  Google Scholar 

  • Trapeznikova, S.S., Paskhina, T.S.: The isolation, purification and properties of carboxypeptidases (kininases) from human and rabbit blood serum. Biokhimiya 33, 1012–1022 (1968).

    CAS  Google Scholar 

  • Trautschold, I.: Enzyme und Inhibitoren der Bildung und des Abbaues gefäßaktiver Polypeptide (Kinine). Habil.-Schrift Munich 1965.

    Google Scholar 

  • Urbanitz, D., Wiegand, H., Habermann, E.: Zur Frage der Bedeutung des Kininsystems beim thermischen Odem der Rattenpfote. Naunyn-Schmiedeberg’s Arch. 264, 476–493 (1969).

    CAS  Google Scholar 

  • Vane, J.R.: The release and rate of vasoactive hormones in the circulation. Brit. J. Pharmacol. 35, 209–242 (1969).

    CAS  Google Scholar 

  • Vorherr, H., Dimitrow, A., Hüter, J.: Biologische Untersuchungen über den Abbau von Hypertensin durch Blutplasma von nichtschwangeren und schwangeren Frauen. Klin. Wschr. 43, 614–617 (1965).

    PubMed  CAS  Google Scholar 

  • Watanabe, N.: Kininase activity in human blood in normal and pathological conditions. Tohoku J. exp. Med. 92, 63–72 (1967).

    PubMed  CAS  Google Scholar 

  • Watanabe, N., Abe, K., Kumagai, N., Mouri, T., Seki, T., Yoshinaga, K.: Kininase activity in human blood. Tohoku J. exp. Med. 89, 383–386 (1966).

    PubMed  CAS  Google Scholar 

  • Webster, M.E.: Report of the committee on nomenclature for hypotensive peptides. In: Hypotensive Peptides, pp. 648–653. Ed. by E.G. Erdös, N. Back and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Webster, M.E., Pierce, J.V.: The nature of the kallidins released from human plasma by kallikreins and other enzymes. Ann. N.Y. Acad. Sci. 104, 91–105 (1963).

    PubMed  CAS  Google Scholar 

  • Webster, M.E., Skinner, N.S., Jr., Powell, W.J., Jr.: Role of the kinins in vasodilatation of skeletal muscle of the dog. Amer. J. Physiol. 212, 553–558 (1967)

    PubMed  CAS  Google Scholar 

  • Werle, E.: Über Kallidin und Bradykinin. Arch. int. Pharmacodyn. 92, 427–431 (1953).

    PubMed  CAS  Google Scholar 

  • Werle, E.: Kallikrein, kallidin and related substances. In: Polypeptides which affect smooth muscles and blood vessels, pp. 199–209. Ed. by M. Schachter. Oxford 1960.

    Google Scholar 

  • Werle, E., Berek, U.: Über Kallidin. Biochem. Z. 320, 136–145 (1950).

    CAS  Google Scholar 

  • Werle, E., Götze, W., Keppler, A.: Über die Wirkung des Kallikreins auf den isolierten Darm und über eine neue darmkontrahierende Substanz. Biochem. Z. 289, 217–233 (1937).

    CAS  Google Scholar 

  • Werle, E., Grunz, M.: Zur Kenntnis der darmkontrahierenden, uteruserregenden und blutdrucksenkenden Substanz Dk. Biochem. Z. 301, 429–436 (1939).

    CAS  Google Scholar 

  • Werle, E., Kehl, R., Koebke, K.: Über Trypsin, Chymotrypsin, Kallidin und Bradykinin. Biochem. Z. 321, 213–220 (1950).

    PubMed  CAS  Google Scholar 

  • Werle, E., Vogel, R., Göldel, L.F.: Über ein blutdrucksteigerndes Prinzip in Extrakten aus der Glandula submaxillaries der weißen Maus. Arch. exp. Path. Pharmakol. 230, 236–244 (1957).

    CAS  Google Scholar 

  • Wernze, H., Fujii, J.: Hepatische Inaktivierung und pressorische Wirkung von Angiotensin. Z. ges. exp. Med. 140, 128–135 (1966).

    CAS  Google Scholar 

  • Wernze, H., Hosoda, S., Schölkens, B.: Zur vasopressorischen Wirkung und Inaktivierung von Angiotensin bei essentieller und renaler sowie experimenteller Hypertonie. Arch. Klin. Med. 214, 286–305 (1968).

    PubMed  CAS  Google Scholar 

  • Wolf, R.L., Mendlowttz, M., Gitlow, S.E., Naftchi, N.: The metabolism of angiotensin II. Circulat. Res. 11, 195–208 (1962).

    PubMed  CAS  Google Scholar 

  • Wood, J.E.: Genetic control of neutralization of angiotensin and its relationship to essential hypertension. Circulation 25, 225–230 (1962).

    PubMed  CAS  Google Scholar 

  • Yamafuji, K., Carrara, M.C.: Studies on the kininase activity of rabbit polymorphonuclear leucocytes. Fed. Proc. 27, 533 (1968).

    Google Scholar 

  • Yang, H.Y.T., Erdös, E.G.: Second kininase in human blood plasma. Nature (Lond.) 215, 1402–1403 (1967).

    CAS  Google Scholar 

  • Yang, H.Y.T., Erdös, E.G.: Angiotensinase C, characterization and chemical assay. Fourth International Congress on Pharmacology Abstracts, p. 217. Basel 1969a.

    Google Scholar 

  • Yang, H.Y.T., Erdös, E.G.: Fluorometric assay of angiotensinase C activity. Pharmacologist 11, 217 (1969b).

    Google Scholar 

  • Yang, H.Y.T., Erdös, E.G., Levin, Y.: A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. biophys. Acta (Amst.) 214, 374–376 (1970d).

    CAS  Google Scholar 

  • Yang, H.Y.T., Erdös, E.G., Levin, Y.: Characterization of a dipeptide hydrolase. (Kininase II; Angiotensin I converting enzyme). J. Pharmacol. exp. Ther. (in press) (1970e).

    Google Scholar 

  • Yang, H.Y.T., Erdös, E.G., Chiang, T.S.: New enzymatic route for the inactivation of angiotensin. Nature (Lond.) 218, 1224–1226 (1968).

    CAS  Google Scholar 

  • Yang, H.Y.T., Erdös, E.G., Jenssen, T.A., Rodgers, J.G.: Characteristics of an enzyme that inactivates angiotensin II (angiotensinase C). Biochem. Pharmacol. 19, 1201 (1970a).

    CAS  Google Scholar 

  • Yang, H.Y.T., Erdös, E.G., Jenssen, T.A., Levin, Y.: Characterization of an angiotensin I converting enzyme. Fed. Proc. (in press) (1970c).

    Google Scholar 

  • Yang, H.Y.T., Jenssen, T.A., Erdös, E.G.: Conversion of angiotensin I by a kininase preparation. Clin. Res. 18, 88 (1970b).

    Google Scholar 

  • Yman, L., Kulling, B.: An aminopeptidase from human serum specific for hydrolysis of α-L-dicarboxylic amino acid residues. I. Purification from retroplacental serum by preparative polyacrylamide-gel electrophoresis. Acta Pharm. Suecica 6, 561–568 (1969).

    CAS  Google Scholar 

  • Yman, L., Kulltng, B., Barth, T.: An aminopeptidase from human serum specific for hydrolysis of α-L-dicarboxylic amino acid residues. II. Some properties and its relationship to the serum angiotensinase activity. Acta Pharm. Suecica 6, 569–578 (1969).

    CAS  Google Scholar 

  • Zachariae, H., Malmquist, J., Oates, J.A.: Kininase in human polymorphonuclear leukocytes. Life Sci. 5, 2347–2355 (1966).

    PubMed  CAS  Google Scholar 

  • Zuber, H.: Purification and properties of a new carboxypeptidase from citrus fruit. Nature (Lond.) 201, 613 (1964).

    CAS  Google Scholar 

  • Zuber, H.: Observations on the use of enzymes in the analysis of peptides. In: Peptides, p. 189. Ed. by L. Zervas. Oxford: Pergamon Press 1966.

    Google Scholar 

  • Zuber, H., Jaques, R.: Isolierung von Bradykinin aus Rinderplasma nach Einwirkung von Schlangengift (Bothrops jararaca). Helv. chim. Acta 43, 1128–1130 (1960).

    CAS  Google Scholar 

  • Zwanzig, M., Oelkers, W.: Untersuchungen über die pH-Abhängigkeit, die Hemmbarkeit und Reaktivierbarkeit von Angiotensin II und Angiotensin II-Amid spaltenden Enzymen des menschlichen Plasmas. Z. klin. Chem. u. klin Biochem. 7, 253–258 (1969).

    CAS  Google Scholar 

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Erdös, E.G. (1971). Enzymes that Inactivate Vasoactive Peptides. In: Brodie, B.B., Gillette, J.R., Ackerman, H.S. (eds) Concepts in Biochemical Pharmacology. Handbook of Experimental Pharmacology / Handbuch der experimentellen Pharmakologie, vol 28 / 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-65177-9_36

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  • DOI: https://doi.org/10.1007/978-3-642-65177-9_36

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