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Bradykinin, Kallidin and Kallikrein pp 156–192Cite as

Proteolytic Enzymes as Kininogenases

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Abstract

The discovery of enzymes, other than kallikreins, which release kinins from blood plasma was made by Rocha e Silva et al. (1949a) when they observed the formation of bradykinin by adding either trypsin or Bothrops jararaca venom to plasma globulins One year later Beraldo (1950a, b) reported the kininliberating activity of fibrinolysin (plasmin), when it was incubated with plasma globulins precipitated by half saturation with ammonium sulfate. A cysteineactivated protease secreted by Clostridium histolyticum was next shown to release from fraction IV-4 of bovine plasma a bradykinin-like polypeptide (J L Prado et al., 1956). This group of kinin-releasing enzymes, kininogenases, has been growing up to the present time and now includes several proteolytic enzymes.

The financial support of this work by the National Institutes of Health (Grant No. HE 09267), Fundação de Amparo à Pesquisa do Estado de São Paulo and CAPES/BNDE/BID Project, is gratefully acknowledged.

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References

  • Andrade, S. O., Rocha EVA, M.: Purification of bradykinin by ion-exchange chromatography. Biochem. J. 64, 701 (1956).

    PubMed  CAS  Google Scholar 

  • Anson, M. L.: The extinction of pepsin, trypsin, papain and cathepsin with hemoglobin. J. gen. Physiol. 22, 79 (1938).

    Article  PubMed  CAS  Google Scholar 

  • Arman, C. G.: Origin of bradykinin. Proc. Soc. exp. Biol. (N.Y.) 79, 356 (1952). Chem. Abstr. 46, 5625f (1952).

    Google Scholar 

  • Arman, C. G.: Interrelationship among some peptide precursors. In: Polypeptides which stimulate plain muscle, p. 103, ed. by J. H. GADDUM. London 1955.

    Google Scholar 

  • Arrau1, R. P., Shelley, W. B.: The role of proteolytic enzymes in the production of pruritus in man. J. invest. Derm. 25, 341 (1955).

    Google Scholar 

  • Arrau1, R. P., Shelley, W. B.: The nature of itching in dermatitic skin Ann. intern. Med. 49, 900 (1958).

    Google Scholar 

  • Babel, I., Stella, R. C. R., Prado, E. S.: Action of horse urinary kallikrein on synthetic derivatives of bradykinin. Ciencia Cult. (S. Paulo) 19, 395 (1967).

    Google Scholar 

  • Back, N., Steger, R.: Effect of inhibitors on kinin-releasing activity of proteases. Fed. Proc. 27, 96 (1968).

    PubMed  CAS  Google Scholar 

  • Beraldo, W. T.: Formation of bradykinin in anaphylactic and peptone shock. Amer. J. Physiol. 163, 283 (1950a).

    PubMed  CAS  Google Scholar 

  • Beraldo, W. T.: Bradykinin formation by the action of peptone and fibrinolysin on plasma globulins in vitro. Ciencia Cult. (S. Paulo) 2, 300 (1950b).

    Google Scholar 

  • Bhoola, K. D., Calle, J. D., Schachter, M.: The effect of bradykinin, serum kallikrein and other endogenous substances on capillary permeability in the guinea pig. J. Physiol. (Lond.) 152, 75 (1960).

    CAS  Google Scholar 

  • Bhoola, K. D., Yt, R. M. M., Morley, J., Schachter, M.: Release of kinin by an enzyme in the accessory sex glands of the guinea pig. J. Physiol. (Lond.) 163, 269 (1962).

    CAS  Google Scholar 

  • Brandi, C. M. W., Mendes, J., Paiva, A. C. M., Prado, E. S.: Proteolysis of salmine by horse urinary kallikrein. Biochem. Pharmacol. 14, 1665 (1965).

    Article  PubMed  CAS  Google Scholar 

  • Brandi, C. M. W., Roncada, M. J., Prado, E. S., Prado, J. L.: Observations on the hydrolysis of salmine by kallikreins. In: Internat. Symposium on Vasoactive Polypeptides: Bradykinin and Related Kinins, p 135, ed. by M. Rocha E Silva and H. A. Rothschild Silo Paulo 1967.

    Google Scholar 

  • Braun-Menendez, E., Fasciolo, J. C., Leloir, L. F., Muoz, J. M., Taquini, A. C.: Relationship between hypertensin and pepsitensin. Rev. Soc. argent. Biol. 19, 304 (1943).

    Google Scholar 

  • Braun-Menendez, E., Fasciolo, J. C., Leloir, L. F., Muoz, J. M., Taquini, A. C.: Renal hypertension. Springfield, Ill. 1946.

    Google Scholar 

  • Brocklehurst, W. E., Mawer, G. E.: The purification of a kininogen from human plasma. Brit. J. Pharmacol. 27, 256 (1966).

    PubMed  CAS  Google Scholar 

  • Carlini, E. A., Huggins, C. G.: Enzymic conversion of valines-angiotensin-I into an oxytocic principle by impure preparations of alpha-amylase. Biochem. Pharmacol. 11, 171 (1962).

    Article  PubMed  CAS  Google Scholar 

  • Carlini, E. A., Picarelli, Z. P., Prado, J. L.: Pharmacological activity of hypertensin I and its conversion into hypertensin II. Bull. Soc. Chim. biol. (Paris) 40, 1825 (1958).

    CAS  Google Scholar 

  • Cormia, F. E., Dougherty, J. W.: Proteolytic activity in development of pain and itching: Cutaneous reactions to bradykinin and kallikrein. J. invest. Derm. 35, 21 (1960).

    PubMed  CAS  Google Scholar 

  • Cormia, F. E., Dougherty, J. W., Unrau, S. A.: Proteolytic activity in dermatoses. J. invest. Derm. 28, 425 (1957).

    PubMed  CAS  Google Scholar 

  • Corrado, A. P.: Considerations upon the participation of bradykinin and analogous peptides on the hemodynamic effects produced by proteolytic enzymes. Thesis, Faculdade de Medicina, Ribeirilo Preto (1964).

    Google Scholar 

  • Corrado, A. P., Reis, M. L., Carvalllo, I. F., Diniz, C. R.: Bradykininogen and bradykinin in the cardiovascular shock produced by proteolytic enzymes. Biochem. Pharmacol. 15, 959 (1966).

    Article  PubMed  CAS  Google Scholar 

  • Croxatto, H.: Active polypeptides formed by pepsin. In: Polypeptides which stimulate plain muscle, p. 92, ed. by J. H. Gaddum. Edinburgh and London 1955.

    Google Scholar 

  • Croxatto, H., Barnafi, L., Rojas, G., Reyes, A., Infante, A.: Antidiuretic and oxytocic substances liberated by the digestion of plasmatic proteins with pepsin. Nature (Lond.) 171, 82 (1953).

    Article  CAS  Google Scholar 

  • Croxatto, H., Rojas, G., Barnafi, L.: Separable oxytocic and pressor actions of pepsitensin. Bol. Soc. Biol. Santiago 8, 84 (1950).

    Google Scholar 

  • Croxatto, H., Rojas, G., Barnafi, L.: The liberation of an antidiuretic factor by the hypertensinogen pepsin reaction. Acta physiol. lat.-amer. 1, 178 (1951).

    PubMed  CAS  Google Scholar 

  • Dengler, H.: Untersuchungen über Pepsitensin. Z. ges. exp. Med. 127, 153 (1956). Biol. Abstr. 31, 31581 (1957).

    Google Scholar 

  • Drniz, C. R., Pereira, A. A., Barroso, J., Mares-Guta, M.: On the specificity of urinary kallikreins. Biochem. biophys. Res. Commun. 21, 448 (1965).

    Google Scholar 

  • Drniz, C. R., Pereira, A. A., Barroso, J., Mares-Guta, M.: Studies of the specificity of kinin-forming enzymes: The inhibition of the kininogenic activity of trypsin and kallikreins by model compounds. In: Hypotensive peptides, p. 175, ed. by E. G. Erdös, N. Back and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Elliott, D. F.: Bradykinin and its mode of release. Ann. N.Y. Acad. Sci. 104, 35 (1963).

    Article  CAS  Google Scholar 

  • Elliott, D. F., Horton, E. W., Lewis, G. P.: Biological activity of pure bradykinin J Physiol. (Lond.) 150, 6P (1959a).

    Google Scholar 

  • Elliott, D. F., Horton, E. W., Lewis, G. P.: Actions of pure bradykinin. J. Physiol. (Lond.) 153, 473 (1960c).

    CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Elliott, D. F., Lewis, G. P., Horton, E. W.: The isolation of bradykinin, A plasma kinin from ox blood. Biochem. J. 74, 15P (1959b). 188 J.

    Google Scholar 

  • L. Prado, Elliott, D. F., Lewis, G. P., Horton, E. W.: The structure of bradykinin. Biochem. J. 76, 16P (1960a).

    Google Scholar 

  • L. Prado, 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 (1960b).

    Google Scholar 

  • L. Prado, Elliott, D. F., Lewis, G. P., Horton, E. W.: The isolation of bradykinin, a plasma kinin from ox blood. Biochem. J. 78, 60 (1961).

    Google Scholar 

  • L. Prado, Elliott, D. F., Smyth, D. C.: A new kinin from ox blood. Biochem. J. 87, 21P (1963).

    Google Scholar 

  • Endo, R. M., Santos, M., Carlini, E. A.: Effects of a crystalline proteinase from Bacillussubtilis (Nagarse) on angiotensins I and II. Experientia (Basel) 22, 757 (1966).

    Article  CAS  Google Scholar 

  • Erdös, E. G.: Hypotensive peptides: Bradykinin, kallidin and eledoisin. Advanc. Pharmacol. 4, 1 (1966).

    Article  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 (1963).

    Article  Google Scholar 

  • Erdös, E. G., Ague, L. L., Miwa, I.: Kallikrein in granules of the submaxillary gland. Biochem. Pharmacol. 17, 667 (1968).

    Article  PubMed  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Fasciolo, J. C., Halvorsen, K.: Specificity of mammalian kallidinogen. Amer. J. Physiol. 207, 901 (1964).

    PubMed  CAS  Google Scholar 

  • Frey, E. K., Kraut, H., Werle, E.: Kallikrein (Padutin), p. 107. Sutttgart 1950.

    Google Scholar 

  • Gaddum, J. H.: Summary of meeting. In: Polypeptides which affect smooth muscles and blood vessels, p. 329, ed. by M. Scrachter. Edinburgh and London 1960.

    Google Scholar 

  • Glazer, A. N.: Esteratic reactions catalyzed by subtilisins. J. biol. Chem. 242, 433 (1967).

    PubMed  CAS  Google Scholar 

  • Gomes, F. P.: A slow contracting substance in normal human urine. Brit. J. Pharmacol. 10, 200 (1955).

    PubMed  CAS  Google Scholar 

  • Greenbaum, L. M., Hosoda, T.: Studies on the isolation of bradykininogen. Biochem. Pharmacol. 12, 325 (1963).

    Article  PubMed  CAS  Google Scholar 

  • Greenbaum, L. M., Yamafuji, K., Hosoda, T.: Studies on the peptic degradation of bovine bradykininogen. Biochem. Pharmacol. 14, 411 (1965).

    Article  PubMed  CAS  Google Scholar 

  • Gross, P., Labouesse, B.: La clostripaine, protéase de Clostridium histolyticum. II. Specificité. Bull. Soc. Chim. biol. (Paris) 42, 559 (1960).

    Google Scholar 

  • Habermann, E.: Über Zusammenhänge zwischen esterolytischen und pharmakologischen Wirkungen von Jararacagift, Kallikrein und Thrombin. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 236, 492 (1959).

    Article  CAS  Google Scholar 

  • Habermann, E.: Diisopropylfluorophosphat-Hemmung esterolytischer und pharmakologischer Wirkungen von Kallikrein und Schlangengiften. Naturwissenschaften 47, 111 (1960).

    Article  CAS  Google Scholar 

  • Habermann, E.: Enzymatic kinin release from purified kininogen and from low molecular compounds. Biochem. Pharmacol. 14, 1393 (1965).

    Google Scholar 

  • Habermann, E.: Enzymatic kinin release from kininogen and from low molecular compounds. In: Hypotensive peptides, p. 116, ed. by E. G. Erdös, N. Back and F. Sicuterl Berlin-HeidelbergNew York: Springer 1966a.

    Google Scholar 

  • Habermann, E.: Strukturaufklärung kininliefernder Peptide aus Rinderserum-Kininogen. Naunyn Schmiedebergs Arch. exp. Path. Pharmak. 253, 474 (1966b).

    CAS  Google Scholar 

  • Habermann, E., Blennemann, G.: Über Substrate und Reaktionsprodukte der kininbildenden Enzyme Trypsin, Serum und Pankreaskallikrein sowie von Crotalusgift. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 249, 357 (1964).

    Article  CAS  Google Scholar 

  • Habermann, E., Blennemann, G., Müller, B.: Charakterisierung und Reinigung peptischer kininliefernder Fragmente (P.KF) sowie von „Pepsitocin“ aus Rinderserum-Kininogen. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 253, 444 (1966).

    CAS  Google Scholar 

  • Habermann, E., Kum, W.: Beiträge zur Biochemie und Pharmakologie eines Serumkallikreins. Naunyn Schmiedebergs Arch. exp. Path. Pharmak. 250, 253 (1965).

    Article  Google Scholar 

  • Habermann, E., Kum, W., Rosenbusch, G.: Partielle Reinigung und einige Eigenschaften eines Kininogens aus Rinderblut. Hoppe-Seylers Z. physiol. Chem. 332, 121 (1963).

    CAS  Google Scholar 

  • Habermann, E., Müller, B.: Zur enzymatischen Spaltung peptischer kininliefernder Fragmente (PKF) sowie von Rinderserumkininogen. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 253, 464 (1966).

    CAS  Google Scholar 

  • Habermann, E., Scriuck, S.: Einige Beziehungen zwischen „Pepsitocin“ und Plasmakininen. Naturwissenschaften 51, 61 (1964).

    Google Scholar 

  • Hagihara, B.: Bacterial and mold proteases. In: The enzymes, 2nd ed., vol. 4, pt. A, p. 193, ed. by P. D. Boyer, H. Lardy, and K. Myrback. New York and London 1960.

    Google Scholar 

  • Hagihara, B., Matsubara, H., Nakai, M., Okunuki, K.: Crystalline bacterial proteinase. I. Preparation of crystalline proteinase of Bacillus subtilis. J. Biochem. (Tokyo) 45, 185 (1958a).

    CAS  Google Scholar 

  • Hagihara, B., Nakai, M., Matsubara, H., Komaki, T., Yonetani, T., Okunuki, K.: Crystalline bacterial proteinase. III. Comparison of crystalline proteinase of Bacillus subtilis with crystalline trypsin. J. Biochem. (Tokyo) 45, 305 (1958b).

    CAS  Google Scholar 

  • Hamberg, U., Rumpus, F. M., Page, I. H.: Isolation and amino acid composition of bradykinin released by venom of Bothrops jararaca from bovine plasma. Biochim. biophys. Acta (Amst.) 52, 533 (1961).

    Article  CAS  Google Scholar 

  • Hamberg, U., RochaE, Silva, M.: On the nature of the bond split by agents releasing bradykinin from plasma proteins. Proc. XX. Internat. Physiol. Congr., p. 390. Brussels 1956.

    Google Scholar 

  • Hamberg, U., Rocha E, Silva, M.: Release of bradykinin as related to the esterase activity of trypsin and of the venom of Bothrops jararaca. Experientia (Basel) 13, 489 (1957a).

    Article  CAS  Google Scholar 

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

    Google Scholar 

  • Hartley, B. S.: Proteolytic enzymes. Ann Rev. Biochem. 29, 45 (1960).

    Article  PubMed  CAS  Google Scholar 

  • Henriques, O. B., Kauritcheva, N., Kuznetsova, V., Astrakan, M.: Substrates of kininreleasing enzymes isolated from horse plasma. Nature (Lond.) 215, 1200 (1967).

    Article  CAS  Google Scholar 

  • Henriques, O. B., Lavras, A. A. C., Fichman, M., Picarelli, Z. P.: Plasma enzymes that release kinins. Biochem. Pharmacol. 15, 31 (1966).

    Article  PubMed  CAS  Google Scholar 

  • Henriques, O. B., Picarelli, Z. P., Ferrai D., Oliveira, M. C.: Partial purification of the plasma substrate for the bradykinin-releasing enzyme from the venom of Bothrops jararaca. Biochem. Pharmacol. 11, 707 (1962).

    Article  PubMed  CAS  Google Scholar 

  • Hochstrasser, K., Werle, E.: Über kininliefernde Peptide aus pepsinverdauten Rinderplasmaproteinen. Hoppe-Seylers Z. physiol. Chem. 348, 177 (1967).

    CAS  Google Scholar 

  • Holdstock, D. J., Mathias, A. P., Seaachter, M.: A comparative study of kinin, kallidin and bradykinin. Brit. J. Pharmacol. 12, 149 (1957).

    PubMed  CAS  Google Scholar 

  • Hopsu, V. K., Mäkinen, K. K., Glenner, G. G.: Characterization of aminopeptidase B: substrate specificity and affector studies. Arch. Biochem. 114, 567 (1966).

    Article  PubMed  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Huggins, C. G., Pavesi, L., Arias, F.: The enzymatic formation of the vasopressor polypeptide substance A by a crystalline enzyme of Bacillus subtilis. Biochem. Pharmacol. 13, 697 (1964).

    Article  PubMed  CAS  Google Scholar 

  • Huggins, C. G., Thampi, S. N.: Vasopressor principle liberated by a crystalline enzyme of “ Bacillus subtilis” (Nagarse) from heat treated horse plasma. In: Internat. Symposium on Vaso-active Polypeptides: Bradykinin and Related Kinins, p. 127, ed. by M. ROCHA E SILVA and H. A. Rothschild São Paulo 1967.

    Google Scholar 

  • Huggins, C. G., Walaszek, E. J.: Large scale preparation and purification of the vasopressor polypeptide, substance A. J. med. pharm. Chem. 5, 183 (1962).

    Article  CAS  Google Scholar 

  • Hunt, J. A., Ottensen, M.: A comparison of three proteinases from various strains of Bacillus subtilis. Biochim. biophys. Acta (Amst.) 48, 412 (1961).

    Article  Google Scholar 

  • Iwanaga, S., Sato, T., Mizushima, Y., Suzuus, T.: Studies on snake venoms. XVII. Properties of the bradykinin releasing enzyme in the venom of Agkistrodon halys blomhof fii. J. Biochem. (Tokyo) 58, 123 (1965).

    CAS  Google Scholar 

  • Jacobsen, S.: Substrates for plasma kinin-forming enzymes in human, dog and rabbit plasmas. Brit. J. Pharmacol. 26, 403 (1966a).

    PubMed  CAS  Google Scholar 

  • Jacobsen, S.: Separation of two different substrates for plasma kinin-forming enzymes. Nature (Lond.) 210, 98 (1966b).

    Article  CAS  Google Scholar 

  • Jaques, R., Scuar, B.: Fermentwirkungen an isolierten glattmuskulären Organen und Zellen, unter besonderer Berücksichtigung proteolytischer Fermente. Helv. physiol. pharmacol. Acta 15, 134 (1957).

    CAS  Google Scholar 

  • Kato, H., Nagasawa, S., Suzuki, T.: Relationship between tertiary structure and kinin yielding ability of bovine kininogen. Biochem. biophys. Res. Commun. 27, 163 (1967).

    CAS  Google Scholar 

  • Kimmel, J. R., Smith, E. L.: Crystalline papain. I. Preparation. specificity and activation. J. biol. Chem. 207, 515 (1954).

    CAS  Google Scholar 

  • Kramer, C., Prado, E. S., Prado, JL: Inhibition by ions of the esterolytic activity of horse urinary kallikrein. Med. Pharmacol. exp. (Basel) 15, 389 (1966).

    Article  CAS  Google Scholar 

  • Kramer, C., Whitaker, J. R.: Ficus enzymes. II. Properties of the proteolytic enzymes from the latex of Ficus carica variety Kadota. J. biol. Chem. 239, 2178 (1964).

    PubMed  CAS  Google Scholar 

  • Kraut, H., Frey, E. K., Paver, E.: Über ein nues Kreislaufhormon. II. Mitt. Hoppe Seylers Z. physiol. Chem. 175, 97 (1928).

    Article  CAS  Google Scholar 

  • Kunitz, M.: Crystalline soybean trypsin inhibitor. II. General properties. J. gen. Physiol. 30, 291 (1947).

    Article  PubMed  CAS  Google Scholar 

  • Labouesse, B.: L’hydrolyse du glucagon par la clostripaine. Bull. Soc. Chim. Biol. (Paris) 42, 1293 (1960).

    CAS  Google Scholar 

  • Labouesse, B.: Gross, P.: La clostripaine, protéase de Clostridium histolyticum. I. Purification et activation par les thiols. Bull. Soc. Chim. biol. (Paris) 42, 543 (1960).

    CAS  Google Scholar 

  • Lewis, J. P.: Formation of plasma kinins by plasmin. J. Physiol. (Lond.) 140, 285 (1959).

    Google Scholar 

  • Lewis, J. P.: Active polypeptides derived from plasma proteins. Physiol. Rev. 40, 647, cf. p. 657 (1960).

    Google Scholar 

  • Mares-Guta, M., Drsiz, C. R.: The specificity of kallikreins, as studied with model compounds. In: Internat. Symposium on Vasoactive Polypeptides: Bradykinin and Related Kinins, p. 149, ed. by M. Rochae Silva and H. A. Rothschild. São Paulo 1967.

    Google Scholar 

  • Marrland, F. S., Smith, E. L.: Subtilisin BPN’. VII. Isolation of cyanogen bromide peptides and the complete amino acid sequence. J. biol. Chem. 242, 5198 (1967).

    Google Scholar 

  • Matsubara, H., Hagihara, B., Nakai, M., Koma, T., Yonetani, T., Okunui, K.: Crystalline bacterial proteinase. II. General properties of crystalline proteinase of Bacillus subtilis N’. J. Biochem. (Tokyo) 45, 251 (1958).

    CAS  Google Scholar 

  • Monier, R., Litwack, G., Sorlo, M., Labouesse, B.: Les enzymes protéolytiques de Clostridium histolyticum. Influence de la complexone III et du calcium sur la stabilité de deux de ces enzymes. Biochim. biophys. Acta (Amst) 18, 71 (1955).

    Article  CAS  Google Scholar 

  • Moss, J. N., Frazier, C. V., Martin, G. J.: Bromelains. The pharmacology of the enzymes. Arch. int. Pharmacodyn. 145, 166 (1963).

    CAS  Google Scholar 

  • Nomoto, M., Narahashi, Y.: Proteolytic enzyme of Streptomyces griseus. I. Purification of protease of Streptomyces griseus. Rikagaku Kenkyusho Hokoku 34, 381 (1958). I II. Homogeneity of highly purified enzyme. Rikagaku Kenkyusho Hokoku 34, 393 (1958). Cf. Chem. Abstr. 54, 688d (1960).

    Google Scholar 

  • Nomoto, M., Narahashi, Y.,Murauami, M.: A proteolytic enzyme of Streptomyces griseus. VII. Hydrolysis of synthetic substrate by St. griseus protease (specificity of St. griseus protease). Rikagaku Kenkyusho Hokoku 35, 261 (1959). Cf. Chem. Abstr. 54, 212–691 (1960).

    Google Scholar 

  • Okunukh, K., Matsubara, H., Nishhmura, S., Hagihara, B.: Specificity of crystalline bacterial proteinase. J. Biochem. (Tokyo) 43, 857 (1956).

    Google Scholar 

  • Paiva, A. C. M.: Comparative study of pepsitensin and hypertensin, p. 30. Thesis, Escola Paulista de Medicina, São Paulo (1954).

    Google Scholar 

  • Picarelli, Z. P., Henriques, O. B., Oliveira, M. C. F.: Potentiation of bradykinin action on smooth muscle by cysteine. Experientia (Basel) 18, 77 (1962).

    Article  CAS  Google Scholar 

  • Pierce, J. V.: Structural features of plasma kinins and kininogens. Fed. Proc. 27, 52 (1968).

    PubMed  CAS  Google Scholar 

  • Pierce, J. V., Webster, M. E.: The purification and some properties of two different kallidinogens from human plasma. In: Hypotensive peptides, p. 130, ed. by E. G. Erdös, N. Back, and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Pisano, J. J.: Studies on the structure of the major kinin in wasp venom. In: Internat. Symposium on Vasoactive Polypeptides: Bradykinin and Related Kinins, p. 35, ed. by M. Rocha E Silva and H. A. Rothschild. Sao Paulo 1967.

    Google Scholar 

  • Pisano, J. J., Tamura, Z., Ftrano, E., Udenfriend, S.: Vasoactive peptides in wasp venom. Fed. Proc. 24, 488 (1965).

    Google Scholar 

  • Prado, E. S., Prado, J. L.: Partial purification of a plasma kinin-forming enzyme from horse urine. Experientia (Basel) 17, 31 (1961).

    Article  CAS  Google Scholar 

  • Prado, E. S., Prado, J. L., Brandi, C. M. W.: Further purification and some properties of horse urinary kallikrein. Arch. int. Pharmacodyn. 137, 358 (1962).

    CAS  Google Scholar 

  • Prado, E. S., Stella, R. C. R., Roncada, M. J., Prado, J. L.: Action of horse urinary kallikrein on arginine and lysine-peptides. In: Internat. Symposium on Vasoactive Polypeptides: Bradykinin and Related Kinins, p. 141, ed. by M. Rocha E Silva and H. A. Rothschild São Paulo 1967.

    Google Scholar 

  • Prado, J. L.: Kininogenases, plasmakinin-liberating enzymes. Ciencia Cult. (S. Paulo) 14, 231 (1962).

    Google Scholar 

  • Prado, J. L.: Considerations upon the enzymic specificities of kininogenases. Acta physiol. lat.-amer. 14, 215 (1964).

    PubMed  CAS  Google Scholar 

  • Katchburian, A. V., Mendes, J., Prado, E. S.: Ions and the kininogenic activity of horse urinary kallikrein. Acta physiol. lat.-amer. 15, 386 (1965 a).

    Google Scholar 

  • Mendes, J.: Unpublished observations (1965).

    Google Scholar 

  • Mendes, J., Rosa, R. C.: On the kininogenic activity of ficin, with a note on papain. An. Acad. bras. Cien. 37, 295 (1965b).

    Google Scholar 

  • Mendes, J., Stella, R. C. R.: Crystalline ficin and papain as kinin-forming enzymes. In: Internat. Symposium on Vasoactive Polypeptides: Bradykinin and Related Kinins, p. 192, ed. by M. Rocha E Silva and H. A. Rothschild. São Paulo 1967.

    Google Scholar 

  • Monter, R., Prado, E. S., Fromageot, C.: Pharmacologically active polypeptide formed from blood globulin by a cysteine-activated protease from Clostridium histolyticum. Biochim. biophys. Acta (Amst) 22, 87 (1956).

    Article  Google Scholar 

  • Prado, E S: Plasmakinin liberation by clostripaine. An. Acad. bras. Cien. 34, 51 (1962).

    CAS  Google Scholar 

  • Prado, E S, Brandi, C. M. W., Katchburian, A. V.: Some properties of highly purified horse urinary kallikrein. Ann. N.Y. Acad. Sci. 104, 186 (1963).

    Article  PubMed  CAS  Google Scholar 

  • Prado, E S, Jurkiewicz, A.: On the liberation of plasmakinin/s by a crystalline protease from B. subtilis (Nagarse). Ciencia Cult. (S. Paulo) 14, 223 (1962).

    Google Scholar 

  • Prado, E S, Jurkiewicz, A.: Crystalline bacterial proteinase from B. subtilis (Nagarse) as a new kininogenase. Arch. int. Pharmacodyn. 147, 53 (1964).

    CAS  Google Scholar 

  • Prado, J. L., Tamura, Z., Fubano, E., Pisano, J. J., Udenfriend, S.: Characterization of kinins in wasp venom. Biochem. Pharmacol. 14, 1397 (1965 c).

    Google Scholar 

  • Prado, J. L., Tamura, Z., Fubano, E., Pisano, J. J., Udenfriend, S.: Characterization of kinins in wasp venom. In: Hypotensive peptides, p. 93, ed. by E. G. Erdös, N. Back, and F. Sicuteri. Berlin-Heidelberg-New York: Springer 1966.

    Google Scholar 

  • Reis, M. L., Medeiros, M. C., Rocha E, Silva, M.: Release and destruction of kinins by a proteolytic enzyme (Pronase) derived from a fungus Streptomyces griseus. Abstracts of III. Internat. Pharmacol. Congr., No 485. Sao Paulo 1966.

    Google Scholar 

  • RochaE., Silva, M.: Pharmacology of trypsin. Action on mammalian smooth muscles and isolated heart. Circulatory effects of trypsin. Experiments with a crystalline material. Arch. Inst. biol. (S. Paulo) 10, 93 (1939 a).

    Google Scholar 

  • Rocha E., Silva, M.: Pharmacology of trypsin. Toxicity and circulatory effects on cat and rabbit. Folia clin. biol. (S. Paulo) 11, 70 (1939 b).

    Google Scholar 

  • Rocha E., Silva, M.: Beiträge zur Pharmakolgie des Trypsins. I. Wirkung des Trypsins auf die glatten Muskeln des Dünndarms und die Gebärmutter von Säugetieren. Die Freisetzung von Histamin nach Durchströmung der Meerschweinchenlunge mit Trypsin. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 194, 335 (1940 a).

    Google Scholar 

  • Rocha E., Silva, M.: Beiträge zur Pharmakologie des Trypsins. II. Wirkung des Trypsins auf den Blutkreislauf bei Katze, Kaninchen und Hund. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 194, 351 (1940b).

    Article  Google Scholar 

  • Rocha E., Silva, M.: Tryptic shock. Arch. Inst. biol. (S. Paulo) 12, 155 (1941a).

    Google Scholar 

  • Rocha E., Silva, M.: Concerning the mechanism of anaphylactic and tryptic shock. J. Immunol. 40, 399 (1941b).

    Google Scholar 

  • Rocha E., Silva, M.: Bradykinin, Mechanisms of its release by trypsin and kallikrein. Arch. int. Pharmacodyn. 88, 271 (1951).

    CAS  Google Scholar 

  • Rocha E., Silva, M.: Biochemistry and pharmacology of bradykinin. In: Polypeptides which affect smooth muscles and blood vessels, p. 210, ed. by M. SCHACHTER. Oxford 1960.

    Google Scholar 

  • Rocha E., Silva, M.: Definition of bradykinin and other kinins Biochem. Pharmacol. 10, 3 (1962).

    Google Scholar 

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

    Google Scholar 

  • Rocha E., Beraldo, W. T., Andrade, S. O.: On a new hypotensive and smooth muscle stimulating factor (bradykinin) liberated from plasma globulin by snake venom and by trypsin. Proc. First Internat. Congr. of Biochemistry, p. 119. Cambridge 1949 b.

    Google Scholar 

  • Rocha E., 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 (1949 a).

    Google Scholar 

  • Rocha E., Hamberg, U.: On the nature of the bond split by bradykinin releasing agents. Ciencia Cult. (S. Paulo) 8, 177 (1956).

    Google Scholar 

  • Rocha E., Reis, M. L., Ferreira, S. H.: Release of kinins from fresh plasma under varying experimental conditions. Biochem. Pharmacol. 16, 1665 (1967).

    Article  Google Scholar 

  • Rosenfeld, G.: Hematimetric studies in shock produced by animal venoms. Trypsin, histamine and snake venom. Absorption of fluid by the red blood cells. Proc. Internat. Soc. of Hematology, p. 84. 1950.

    Google Scholar 

  • Schachter, M: Kinins of different origins. Ann. N.Y. Acad. Sci. 104, 108 (1963).

    Article  PubMed  CAS  Google Scholar 

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

    Article  Google Scholar 

  • Schröder, E., Hempel, R.: Bradykinin, kallidin and their synthetic analogues. Experientia (Basel) 20, 529 (1964).

    Article  Google Scholar 

  • Schwert, G. W., Takenaka, Y.: Spectrophotometric determination of trypsin and chymotrypsin. Biochim. biophys. Acta (Amst) 16, 570 (1955).

    Article  CAS  Google Scholar 

  • Sgarbieri, V. C., Gupte, S. M., Kramer, D. E., Whtaker, J. R.: Ficus enzymes. I. Separation of the proteolytic enzymes of Ficus carica and Ficus glabrata latices. J. biol. Chem. 239, 2170 (1964).

    CAS  Google Scholar 

  • Smith, E. L., Markland, F. S., Kasper, C. B., Delange, R. J., London, M., Evans, W. H.: The complete amino acid sequence of two types of subtilisin, BPN’ and Carlsberg. J. biol. Chem. 241, 5974 (1966).

    PubMed  CAS  Google Scholar 

  • Stella, R. C. R.: Study on the liberation of kinins in horse plasma by acid activation or by horse urinary kallikrein. Thesis, Escola Paulista de Medicina, Sao Paulo (1968).

    Google Scholar 

  • Stella, R. C. R., Mendes, J., Prado, J. L.: Identification of kinins liberated from equine plasma by acidification and by addition of horse urinary kallikrein. Ciencia Cult. (S. Paulo) 20, 422 (1968).

    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, p. 149, ed. by E. G. Erdös, N. Back, and F. Sicuteri. BerlinHeidelberg-New York: Springer 1966.

    Google Scholar 

  • Suzuki, T., Iwanaga, S., Sato, T., Nagasawa, S., Kato, H., Yano, M., Horncri, K.: Biochemical properties of kininogens and kinin releasing enzymes. In: Internat. Sym- posium on Vasoactive Polypeptides: Bradykinin and Related Kinins, p. 27, ed. by M. Roc E Siena and H. A. Rothschild. Sâo Paulo 1967.

    Google Scholar 

  • Suzuki, T., Mizushima, Y., Sato, T., Iwanaga, S.: Purification of bovine bradykininogen. J. Biochem. (Tokyo) 57, 180 (1965).

    Google Scholar 

  • Trautschold, I., Werle, E., Zickgraf-Rüdel, G.: Trasylol. Biochem. Pharmacol. 16, 59 (1967).

    Article  CAS  Google Scholar 

  • Trethewie, E. R.: Tissue injury by trypsin. Aust. J. exp. Biol. med. Sci. 20, 49 (1942).

    Article  CAS  Google Scholar 

  • Turba, F., Hetzel, H.: Über ein oxytocisch wirkendes Peptid aus Serumprotein. Biochem. Z. 325, 524 (1954).

    PubMed  CAS  Google Scholar 

  • Walaszek, E. J., Bui AG, R. D., Huggins, C. G.: The characterization of the hypertensive polypeptide substance A. J. Pharmacol. exp. Ther. 138, 139 (1962).

    PubMed  CAS  Google Scholar 

  • Walaszek, E. J., Huggins, C. G.: SubstanceA: A hypotensive polypeptide from fraction IV-4 of plasma protein. J. Pharmacol. exp. Ther. 126, 258 (1959).

    PubMed  CAS  Google Scholar 

  • Weber, C. J., Major, R. H., Lobb, D.: The production of a pressor substance from serum globulin by action of pepsin. Science 96, 44 (1942).

    Article  PubMed  CAS  Google Scholar 

  • Webster, M. E.: Report of the committee on nomenclature for hypotensive peptides. In: Hypotensive peptides, p. 648, ed. by E. G. Erdös, N. Back, and F. Sicuteri. BerlinHeidelberg-New York: Springer 1966.

    Google Scholar 

  • Webster, M. E., Pierce, J. V.: Studies on plasma kallikrein and its relationship to plasmin. J. Pharmacol. exp. Ther. 130, 484 (1960).

    PubMed  CAS  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 (1963).

    Article  PubMed  CAS  Google Scholar 

  • Wells, J. A., Morris, H. C., Dragstedt, C. A.: Significance of histamine in trypsin shock as determined by Benadryl. Proc. Soc. exp. Biol. (N.Y.) 62, 209 (1946).

    CAS  Google Scholar 

  • Werle, E.: Zur Kenntnis des Kallikreins. Angew. Chem. 60, 53 (1948).

    Google Scholar 

  • Werle, E.: Über Plasmakinine. In: Symposium Biologisch aktive Polypeptide, p. 57. Vienna 1962.

    Google Scholar 

  • Werle, E.: Plasma-Kinine. Munch. med. Wschr. 50, 2846 (1963).

    Google Scholar 

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

    CAS  Google Scholar 

  • Werle, E., Däumer, J.: Über das Verhalten des Kallikreins, des Inaktivators aus Lymphdrüsen, der Substanz DK, sowie der Histidindecarboxylase bei der Kataphorese. Biochem. Z. 304, 377 (1940).

    CAS  Google Scholar 

  • Werle, E., Forell, M. M., Maier, L.: Zur Kenntnis der blutdrucksenkenden Wirkung des Trypsins. Naunyn-Schmiedebergs Arch. exp. Path. Pharmak. 225, 369 (1955).

    Article  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 (1937).

    CAS  Google Scholar 

  • Werle, E., Griinz, M.: Zur Kenntnis der darmkontrahierenden, uteruserregenden und blutdrucksenkenden Substanz DK. Biochem. Z. 301, 429 (1939).

    CAS  Google Scholar 

  • Werle, E., Hochstrasser, K.: Versuche zur Isolierung eines niedermolekulären Kininogens. Hoppe Seylers Z. physiol. Chem. 332, 322 (1963).

    CAS  Google Scholar 

  • Werle, E., Kaufmann-Boetsch, B.: Über esteratische Wirkungen von Kallikrein und Trypsin und ihre Hemmung durch Kallikrein und Trypsininhibitoren. Hoppe-Seylers Z. physiol. Chem. 319, 52 (1960).

    CAS  Google Scholar 

  • Werle, E., Kehl, R., Koebke, K.: Über Bradykinin, Kallidin und Hypertensin. Biochem. Z. 320, 372 (1950a).

    PubMed  CAS  Google Scholar 

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

    Google Scholar 

  • Werle, E., Koksten, A.: Der Kallikreingehalt des Harns, des Speichels und des Blutes bei Gesunden und Kranken. Z. ges. exp. Med. 103, 153 (1938).

    CAS  Google Scholar 

  • Werle, E., Maier, L.: Über die chemische und pharmakologische Unterscheidung von Kallikreinen verschiedener Herkunft. Biochem. Z. 323, 279 (1952).

    PubMed  CAS  Google Scholar 

  • Werle, E., Maier, L., Ringelmann, E.: Hemmung von Proteinasen durch Kallikrein-Inaktivatoren. Naturwissenschaften 39, 328 (1952).

    Article  CAS  Google Scholar 

  • Yamura, T., Cormia, F. E.: Studies on human skin protease. J. invest. Derm. 37, 121 (1961).

    PubMed  CAS  Google Scholar 

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  1. J. L. Prado
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  1. Department of Pharmacology, University of Oklahoma Medical Center, Oklahoma City, Oklahoma, USA

    Ervin G. Erdös

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Prado, J.L. (1970). Proteolytic Enzymes as Kininogenases. In: Erdös, E.G., Wilde, A.F. (eds) Bradykinin, Kallidin and Kallikrein. Handbook of Experimental Pharmacology / Handbuch der experimentellen Pharmakologie, vol 25 / 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-46222-1_8

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