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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abdul-Karim, R., Assali, N.S.: Pressor response to angiotonin in pregnant and nonpregnant women. Amer. J. Obstet. Gynec. 82, 246–251 (1961).
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).
Abrams, J.S.: Blood pressure response to the portal infusion of angiotensin II. Surg. Forum 17, 133–134 (1966).
Allwood, M.J., Lewis, G.P.: Bradykinin and forearm blood flow. J. Physiol. (Lond.) 170, 571–581 (1964).
Amundsen, E., Nustad, K.: Kinin-forming and destroying activities of saliva. Brit. J. Pharmacol. 23, 440–444 (1964).
Amundsen, E., Nustad, K.: Kinin-forming and destroying activities of cell homogenates. J. Physiol. (Lond.) 179, 479–88 (1965).
Amundsen, E., Rugstad, H.E.: Influence of some pathogenic bacteria on kinin formation and destruction. Brit. J. Pharmacol. 25, 67–73 (1965).
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.
Armstrong, D., Stewart, J.W.: Spontaneous plasma kinin formation in human plasma collected during labour. Nature (Lond.) 188, 1193 (1960).
Ascheim, R.S., Hammel, E.C., Mearles, R.J., Lubash, G.D.: Human serum, liver and kidney angiotensinases. Biochem. Med. 1, 288–294 (1967).
Bakhle, Y.S.: Conversion of angiotensin I to angiotensin II by cell-free extracts of dog lung. Nature (Lond.) 220, 919–920 (1968).
Bakhle, Y.S., Reynard, A.M., Vane, J.R.: Metabolism of the angiotensins in isolated perfused tissues. Nature (Lond.) 222, 956–959 (1969).
Berger, M., Langhans, J.: Angiotensinase activity in pregnant and nonpregnant women. Amer. J. Obstet. Gynec. 98, 215–228 (1967).
Beuzeville, C.A., Lauson, H.D.: Hepatic clearance of angiotensin from plasma of rats and dogs. Fed. Proc. 24, 524 (1965).
Biron, P.: Les angiotensinase du plasma humain. Rev. Canad. Biol. 26, 43–53 (1967).
Biron, P.: Pulmonary extraction of bradykinin and eledoisin. Rev. Canad. Biol. 27, 75–76 (1968).
Biron, P., Baldus, W.P., Summerskill, W.H.J.: Plasma angiotensinase activity in cirrhosis. Proc. Soc. exp. Biol. (N.Y.) 116, 1074–1077 (1964b).
Biron, P., Campeau, L., David, P.: Fate of angiotensin I and II in the human pulmonary circulation. Amer. J. Cardiol. 24, 544–547 (1969).
Biron, P., Landesman, R., Hunt, J.C.: Plasma angiotensinase activity in human hypertension. Nature (Lond.) 204, 1096 (1964a).
Biron, P., Meyer, P.: Hepatic extraction of angiotensin after carbon tetrachloride intoxication. Rev. Canad. Biol. 27, 277–279 (1968).
Biron, P., Baldus, W.P., Panisset, J.-C.: Removal of angiotensins from the systemic circulation. Canad. J. Physiol. Pharmacol. 46, 175–178 (1968).
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).
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).
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).
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).
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).
Boyd, G.W., Landon, J., Peart, W.S.: Radioimmunoassay for determining plasma-levels of angiotensin II in man. Lancet 1967II, 1002–1005.
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).
Braun-Menéndez, E., Fasciolo, J.C., Leloir, L.F., Muñoz, J.M.: The substance causing renal hypertension. J. Physiol. (Lond.) 98, 283–298 (1940).
Braun-Menéndez, E., Fasciolo, J.C., Leloir, L.F., Muñoz, J.M., Taquini, A.C.: Renal Hypertension. Springfield/Ill.: Charles C. Thomas 1946.
Brunner, H.: Resistenz von verschiedenen Angiotensin-II-Isomeren gegen Inaktivierung durch Plasma oder Nierenhomogenat. Arch. exp. Path. 245, 283–284 (1963).
Brunner, H., Regoli, D.: Unterschiedliche Empfindlichkeit verschiedener Angiotensinderivate gegen Abbau durch Plasma oder Nierenhomogenat. Experientia (Basel) 18, 504–505 (1962).
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).
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).
Centaro, A., Periti, P., Sicuteri, F.: Bradykininogen and bradykininase in blood of women during labour. Settim. med. 51, Suppl. I, 70–76 (1963).
Chamberlain, M.J., Browse, N.L., Gibson, D.G., Gleeson, J.A.: Angiotensin and renoportal anastomosis. Brit. med. J. 2, 1507–1508 (1964).
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).
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).
Cohen, L.A., Gage, J.O., Kokame, G.M., Creech, O., Jr.: Hepatic inactivation of angiotensin. Bull. Tulane med. Fac. 26, 295–298 (1967).
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).
Croxatto, H., Cruzatt, H.: Ineffectiveness of carboxypeptidase B in inhibiting the pressor effect of incubated human plasma. Experientia (Basel) 25, 59–60 (1969).
Croxatto, R., Croxatto, H.: Comparative study of hypertensinase and proteinase activity of blood plasma. Proc. Soc. exp. Biol. (N.Y.) 61, 330–333 (1946).
Cushman, D.W., Cheung, H.S.: A simple substrate for assay of dog lung angiotensin converting enzyme. Fed. Proc. 28, 799 (1969).
Dahlheim, H., Petschauer, K., Thurau, K.: Anreicherung und Charakterisierung der Erythrocytenangiotensinase. Pflügers Arch. 305, 105–117 (1969).
Dengler, H., Reichel, G.: Untersuchungen zur intrazellulären Localisation der Renin-und Hypertensinase-Aktivität. Experientia (Basel) 16, 36–40 (1960).
Deutsch, H.F., Diniz, C.R.: Some proteolytic activities of snake venoms. J. biol. Chem. 216, 17–26 (1955).
Dexter, L.: The hypertensinase content of plasma of normal, hypertensive and nephrectomized dogs. Ann. intern. Med. 17, 447–450 (1942).
Dodson, L.F.: The pressor response to hypertensin in pregnant rats. Brit. J. exp. Path. 38, 635–639 (1957).
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).
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).
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).
Edery, H., Lewis, G.P.: Inhibition of plasma kininase activity at slightly acid pH. Brit. J. Pharmacol. 19, 299–305 (1962).
Effkemann, G., Werle, E.: Die körpereigenen uteruswirksamen und kreislaufaktiven Wirkstoffe im Schwangerenorganismus. Arch. Gynäk. 171, 1–27 (1941).
Elliott, D.F., Lewis, G.P.: Methionyl-lysyl-bradykinin, a new kinin from ox blood. Biochem. J. 95, 437–447 (1965).
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).
Enomoto, T., Mineshita, S., Oh-Ishi, S., Shigei, T.: Kininase activity of stem bromelain. Jap. J. Pharmacol. 17, 331–332 (1967).
Erdös, E.G.: Enzymes that inactive active polypeptides. Biochem. Pharmacol. 8, 112 (1961).
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.
Erdös, E.G.: Hypontensive peptides, bradykinin, kallidin and eledoisin. Advanc. Pharmacol. 4, 1–90 (1966).
Erdös, E.G., Cano, G., Yang, H.Y.T.: Hypotensive effect of Lys9-bradykinin in the guinea pig. Biochem. Pharmacol. 16, 1035–1041 (1967c).
Erdös, E.G., McMennamin, M.A., Wohler, J.R.: Presence of carboxypeptidase B in crude kallikrein (Padutin) preparations. Life Sci. 1, 765–769 (1962).
Erdös, E.G., Miwa, I.: Effect of endotoxin shock on the plasma kallikrein-kinin system of the rabbit. Fed. Proc. 27, 92–95 (1968).
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).
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).
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).
Erdös, E.G., Sloane, E.M.: An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem. Pharmacol. 11, 585–592 (1962).
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).
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).
Erdös, E.G., Wohler, J.R.: Inhibitors of the in vivo enzymatic inactivation of bradykinin and kallidin. Life Sci. 2, 270–274 (1963a).
Erdös, E.G., Wohler, J.R.: Inhibition in vivo of the enzymatic inactivation of bradykinin and kallidin. Biochem. Pharmacol. 12, 1193–1199 (1963b).
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).
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.
Erdös, E.G., Yang, H.Y.T.: An enzyme in microsomal fraction of kidney that inactivates bradykinin. Life Sci. 6, 569–574 (1967).
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.
Erdös, E.G., Yang, H.Y.T., Miwa, I.: Kininases. Hoppe-Seylers Z. physiol. Chem. 349, 928 (1968).
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).
Fasciolo, J.C.: Formation and destruction of plasma kinins. Acta physiol. lat.-amer. 14, 170–179 (1964).
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).
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.
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).
Ferreira, S.H., Vane, J.R.: The detection and estimation of bradykinin in the circulating blood. Brit. J. Pharmacol. 29, 367–377 (1967b).
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).
Frey, E.K., Kraut, H., Werle, E.: Kallikrein Padutin. Stuttgart: Ferdinand Enke 1950.
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.
Garbe, G.: Quantitative Kininogenbestimmung in menschlichem Plasma. Naunyn-Schmiedeberg’s Arch. exp. Path. Pharmak. 256, 112–118 (1967).
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).
Goffinet, J.A., Mulrow, P.J.: Estimation of angiotensin clearance by an in vivo assay. Clin. Res. 11, 408 (1963).
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).
Gollan, F., Richardson, E., Goldblatt, H.: Studies on plant hypertensinase. J. exp. Med. 87, 29–39 (1948).
Greenbaum, L.M., Kim, K.S.: The kinin-forming and kininase activities of rabbit polymorphonuclear leucocytes. Brit. J. Pharmacol. 29, 238–247 (1967).
Greenbaum, L.M., Yamafuji, K.: The in vitro inactivation and formation of plasma kinins by spleen cathepsins. Brit. J. Pharmacol. 27, 230–238 (1966).
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).
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).
Haas, E., Goldblatt, H., Lewis, L., Gipson, E.C.: Angiotensin-protective cofactor. Amer. J. Physiol. 217, 981–987 (1969).
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).
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).
Hamberg, U., Rocha e Silva, M.: Studies on the enzymatic inactivation of bradykinin. Acta physiol. scand. 30, 215–225 (1954).
Hamberg, U., Rocha e Silva, M.: On the release of bradykinin by trypsin and snake venoms. Arch. int. Pharmacodyn. 110, 222–238 (1957).
Harakal, C.D., Collins, D.A.: Plasma hypertensinase in experimental renal hypertension. Circulat. Res. 4, 612–617 (1956).
Hess, R.: Arylamidase activity related to angiotensinase. Biochim. biophys. Acta (Amst.) 99, 316–324 (1965).
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).
Hiwada, K.: Studies on plasma angiotensinases in liver disease. Jap. Circulat. J. 32, 1073–1083 (1968).
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).
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).
Hooper, K.C.: The enzymic inactivation of some physiologically active polypeptides by different parts of the nervous system. Biochem. J. 88, 398–404 (1963).
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).
Hopsu, V.K., Makinen, K.K., Glenner, G.G.: Formation of bradykinin from kallidin-10 by aminopeptidase B. Nature (Lond.) 212, 1271–1272 (1966b).
Horton, E.W.: The estimation of urinary kallikrein. J. Physiol. (Lond.) 148, 267–282 (1959).
Itskovitz, H.D., Dudrick, S.J., Dyrda, I., Murphy, J.J.: Plasma angiotensinase activity in hypertensive patients. Arch. intern. Med. 119, 241–246 (1967).
Itskovitz, H.D., Miller, L.D.: Renal angiotensinase activity. Circulat. Res. 19, 507–513 (1966).
Itskovitz, H.D., Miller, L.D.: Differential studies of angiotensinase activities from several tissue sources. Amer. J. med. Sci. 254, 659–666 (1967).
Itskovitz, H.D., Miller, L.D., Ural, W., Zapp, J., White, R.: Inactivation of angiotensin in shock. Amer. J. Physiol. 216, 5–10 (1969).
Johnson, D.C., Ryan, J.W.: Degradation of angiotensin II by a carboxypeptidase of rabbit liver. Biochim. biophys. Acta (Amst.) 160, 196–203 (1968).
Kelly, K.A., Nyhus, L.M.: Angiotensin and the liver. Amer. J. Physiol. 210, 305–311 (1966).
Kemp, E., Rubin, I.: Removal of angiotensinase from a preparation of renin. Arch. Biochem. Biophys. 96, 56–59 (1962).
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).
Khairallah, P.A., Page, I.H. Plasma angiotensinases. Biochem. Med. 1, 1–8 (1967).
Khairallah, P.A., Page, I.H., Bumpus, F.M., Smeby, R.R.: Angiotensin II: Its metabolic fate. Science 138, 523–525 (1962).
Khairallah, P.A., Page, I.H., Bumpus, F.M., Türker, R.K.: Angiotensin tachyphylaxis and its reversal. Circulat. Res. 19, 247–254 (1966).
Klaus, D.: Untersuchungen über die Angiotensinase im Serum Gesunder und Kranker. Klin. Wschr. 40, 701–702 (1962).
Klaus, D.: Vergleichende Untersuchungen über die Blutdruckwirkung von α-und β-Angiotensin II bei intravenöser Infusion. Klin. Wschr. 44, 1044–1046 (1966).
Klaus, D., Daum, A.: Die Wirkung von Aminopeptidase auf den experimentellen renalen Hochdruck der Ratte. Klin. Wschr. 44, 903–904 (1966).
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).
Klaus, D., Kaffarnik, H., Pfeil, H.: Untersuchungen über die Serum-Angiotensinase I, II. Klin. Wschr. 41, 376–385 (1963).
Kleine, R., Tille, D.: Charakterisierung der Protamin hydrolysierenden Enzymwirkung des Rattenserums. Acta biol. med. germ. 22, 525–535 (1969).
Kokubu, T.: Renal hypertension and angiotensinase. Jap. J. Med. 5, 102–104 (1966).
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).
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).
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).
Krivoy, W., Kroger, D.: The preservation of bradykinin by phenothiazines in vitro. Brit. J. Pharmacol. 22, 329–341 (1964).
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).
Kurtz, A.B., Wachsmuth, E.D.: Identification of plasma angiotensinase as aminopeptidase. Nature (Lond.) 221, 92–93 (1969).
Lagrue, G., Meyer, P.: Dosage biologique de l’angiotensinase plasmatique. Technique et premiers résultats. Path. et Biol. 11, 895–897 (1963).
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).
Leary, W.P., Ledingham, J.G.: Removal of angiotensin by isolated perfused organs of the rat. Nature (Lond.) 222, 959–960 (1969).
Levin, Y., Pecht, M., Goldstein, L., Katchalski, E.: A water-insoluble polyanionic derivative of trypsin. I. Preparation and properties. Biochemistry 3, 1905–1913 (1964).
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).
Lubash, G.D., Bard, R.H., Kline, J.A.: Serum “angiotensinase activity” and female steroidal hormones. Amer. J. med. Sci. 257, 155–163 (1969).
Lubash, G.D., Hammel, E.C., Mearles, R.J.: Serum angiotensinase activity in hypertension. Clin. chim. Acta 18, 439–445 (1967).
Lubash, G.D., Hammel, E.C., Mearles, R.J.: Serum angiotensinase activity in cirrhosis. Amer. J. med. Sci. 255, 105–112 (1968).
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).
Margolis, J., Bishop, E.A.: Interrelations between different mechanisms of release of biologically active peptides from blood plasma. Nature (Lond.) 194, 749–751 (1962).
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).
Matsunaga, M., Saito, N., Kira, J., Ogino, K., Takayasu, M.: Acid angiotensinase as a lysosomal enzyme. Jap. Circulat. J. 33, 541–551 (1969).
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).
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).
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).
Melmon, K.L., Cline, M.J.: Interaction of plasma kinins and granulocytes. Nature (Lond.) 217, 90–92 (1967).
Melmon, K.L., Cline, M.J.: The interaction of leukocytes and the kinin system. Biochem. Pharmacol. 17, Suppl., p. 271–281 (1968).
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).
Methot, A.L., Meyer, P., Biron, P., Lorain, M.P., Lagrue, G., Milliez, P.: Hepatic inactivation of angiotensin. Nature (Lond.) 203, 531–532 (1964).
Mitchell, W.M.: Hydrolysis at arginylproline in polypeptides by clostridiopeptidase B. Science 162, 374–375 (1968).
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).
Morris, R.E.: In discussion. Canad. med. Ass. J. 90, 194 (1964).
Myers, M.G., Robinson, P.R., Morris, R.E.: Relationships of angiotensinase and angiotensin II. Clin. Res. 13, 215 (1965).
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).
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).
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).
Nicolaides, E.D., Dewald, H.A., Craft, M.K.: The synthesis of kinin analogues. Ann. N.Y. Acad. Sci. 104, 15–22 (1963).
Nishimura, H., Sokabe, H.: Inhibition of angiotensinases in the rat plasma and kidney. Jap. Heart J. 9, 494–503 (1968).
Nugent, F.W., Atendido, W.A., Bulan, M.B., MacDonald, A.J.: Kininase activity in experimental pancreatitis. Nature (Lond.) 211, 207–208 (1966).
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).
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).
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).
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).
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).
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).
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).
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).
Page, I.H., McCubbin, J.W., editors: Renal Hypertension. Chicago: Year Book Medical Publishers, Inc. 1968.
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).
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).
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).
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.
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).
Riniker, B.: Recent work on the chemistry and biochemistry of angiotensin II. Metabolism 13, 283–291 (1964).
Riniker, B., Schwyzer, R.: Die sterische Einheitlichkeit des synthetischen Val5-Hypertensin II-Asp1-β-amids. Helv. chim. Acta 44, 658–667 (1961).
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).
Rocha e Silva, M.: Bradykinin — mechanism of its release by trypsin and kallikrein. Arch. int. Pharmacodyn. 88, 271–282 (1951).
Rocha e Silva, M.: The physiological significance of bradykinin. Ann. N.Y. Acad. Sci. 104, 190–210 (1963).
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).
Rugstad, H.E.: Kininase production by some microbes. Brit. J. Pharmacol. 28, 315–323 (1966).
Rugstad, H.E.: Purification of a kinin-inactivating enzyme from cultures of Pseudomonas aeruginosa. Brit. J. Pharmacol. 30, 134–142 (1967a).
Rugstad, H.E.: Characterization of a plasma kinin-inactivating enzyme produced by Pseudomonas aeruginosa. Brit. J. Pharmacol. 30, 425–435 (1967b).
Rugstad, H.E.: Degradation of plasma kinins by an enzyme from Pseudomonas aeruginosa. Brit. J. Pharmacol. 31, 401–406 (1967c).
Ryan, J.W., Roblero, J., Stewart, J.M.: Inactivation of bradykinin in the pulmonary circulation. Biochem. J. 110, 795–797 (1968a).
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).
Saameli, K., Eskes, T.K.A.B.: Bradykinin and cardiovascular system: estimation of half-life. Amer. J. Physiol. 203, 261–265 (1962).
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).
Sambhi, M.P., Barrett, J.D.: Angiotensinase activity in fractionated human plasma and effect of enzyme inhibitors. Clin. Res. 14, 149 (1966).
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).
Sapirstein, L.A., Reed, R.K., Page, E.W.: The site of angiotonin destruction. J. exp. Med. 83, 425–439 (1946).
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.
Schröder, E.: Über Peptidsynthesen. Synthese von Methionyl-Lysyl-Bradykinin, einem Kinin aus Rinderblut. Experientia (Basel) 20, 39 (1964).
Schröder, E., Lübke, K.: The Peptides. Vol. II. New York: Academic Press 1966.
Schwab, J.: Kininases in leucocytes and other tissues. Nature (Lond.) 195, 345–347 (1962).
Seki, I., Jenssen, T.A., Levin, Y., Erdös, E.G.: Active water-insoluble derivative of renin. Nature (Lond.) 225, 864–865 (1970b).
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).
Shimonaeva, E.E.: Some properties of carboxypeptidase N from rabbit blood serum. Vop. med. Khim 13, 105–107 (1967).
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).
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).
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).
Stewart, J.M.: Synthesis and pharmacology of polistes kinin, a bradykinin homolog. Fed. Proc. 27, 534 (1968).
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.
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.
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.
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).
Teger-Nilsson, A.-C.: Degradation of human fibrinopeptides A and B in blood serum in vitro. Acta chem. scand. 22, 3171–3182 (1968).
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).
Trautschold, I.: Enzyme und Inhibitoren der Bildung und des Abbaues gefäßaktiver Polypeptide (Kinine). Habil.-Schrift Munich 1965.
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).
Vane, J.R.: The release and rate of vasoactive hormones in the circulation. Brit. J. Pharmacol. 35, 209–242 (1969).
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).
Watanabe, N.: Kininase activity in human blood in normal and pathological conditions. Tohoku J. exp. Med. 92, 63–72 (1967).
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).
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.
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).
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)
Werle, E.: Über Kallidin und Bradykinin. Arch. int. Pharmacodyn. 92, 427–431 (1953).
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.
Werle, E., Berek, U.: Über Kallidin. Biochem. Z. 320, 136–145 (1950).
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).
Werle, E., Grunz, M.: Zur Kenntnis der darmkontrahierenden, uteruserregenden und blutdrucksenkenden Substanz Dk. Biochem. Z. 301, 429–436 (1939).
Werle, E., Kehl, R., Koebke, K.: Über Trypsin, Chymotrypsin, Kallidin und Bradykinin. Biochem. Z. 321, 213–220 (1950).
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).
Wernze, H., Fujii, J.: Hepatische Inaktivierung und pressorische Wirkung von Angiotensin. Z. ges. exp. Med. 140, 128–135 (1966).
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).
Wolf, R.L., Mendlowttz, M., Gitlow, S.E., Naftchi, N.: The metabolism of angiotensin II. Circulat. Res. 11, 195–208 (1962).
Wood, J.E.: Genetic control of neutralization of angiotensin and its relationship to essential hypertension. Circulation 25, 225–230 (1962).
Yamafuji, K., Carrara, M.C.: Studies on the kininase activity of rabbit polymorphonuclear leucocytes. Fed. Proc. 27, 533 (1968).
Yang, H.Y.T., Erdös, E.G.: Second kininase in human blood plasma. Nature (Lond.) 215, 1402–1403 (1967).
Yang, H.Y.T., Erdös, E.G.: Angiotensinase C, characterization and chemical assay. Fourth International Congress on Pharmacology Abstracts, p. 217. Basel 1969a.
Yang, H.Y.T., Erdös, E.G.: Fluorometric assay of angiotensinase C activity. Pharmacologist 11, 217 (1969b).
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).
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).
Yang, H.Y.T., Erdös, E.G., Chiang, T.S.: New enzymatic route for the inactivation of angiotensin. Nature (Lond.) 218, 1224–1226 (1968).
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).
Yang, H.Y.T., Erdös, E.G., Jenssen, T.A., Levin, Y.: Characterization of an angiotensin I converting enzyme. Fed. Proc. (in press) (1970c).
Yang, H.Y.T., Jenssen, T.A., Erdös, E.G.: Conversion of angiotensin I by a kininase preparation. Clin. Res. 18, 88 (1970b).
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).
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).
Zachariae, H., Malmquist, J., Oates, J.A.: Kininase in human polymorphonuclear leukocytes. Life Sci. 5, 2347–2355 (1966).
Zuber, H.: Purification and properties of a new carboxypeptidase from citrus fruit. Nature (Lond.) 201, 613 (1964).
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.
Zuber, H., Jaques, R.: Isolierung von Bradykinin aus Rinderplasma nach Einwirkung von Schlangengift (Bothrops jararaca). Helv. chim. Acta 43, 1128–1130 (1960).
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).
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1971 Springer-Verlag Berlin · Heidelberg
About this chapter
Cite this chapter
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
Download citation
DOI: https://doi.org/10.1007/978-3-642-65177-9_36
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-65179-3
Online ISBN: 978-3-642-65177-9
eBook Packages: Springer Book Archive