Abstract
Mammalian plasmas contain a number of “serine-active site” trypsin-like proteinases, which participate in blood coagulation, kallikrein-kinin, fibrinolysis and complement systems. The proteinases have an ability to cleave selectively proteins, that is, limited proteolysis, and catalyze the cascade reactions, which involve several sequential transformations of proenzymes to enzymes (Davie et al. 1969). Table i shows the amino acid sequences around the scissile bonds of natural substrates attacked by these proteinases. It has been well known that the amino acid residues preceding the scissile bond, P2 and P3 sites, in the substrates, are of importance for the enzyme-substrate interaction (Blomback, 1970). For instance, a part of the sequence, Asp-Asp-Asp-Lys, which is located in the NH2-terminal portion of trypsinogen, has been known to comprise the substrate recognition sites and specificity sequence for enterokinase (Ottesen, 1967). Similarly, Factor Xa is presumed to recognize the tetrapeptide sequence Ile-Glu-Gly-Arg located close to the cleavage site required for the activation of bovine prothrombin (Magnusson et al. 1975). Based on this idea, several peptidyl-p-nitroanilides, so called “chromogenic substrate”, which suit a specificity requirement of proteinases,
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References
Blombäck, B. (1970) In: The Hemostatic Mechanism in Man and Other Animals (ed. by R. G. Macfarlane), pp. 169–182, Academic Press, New York.
Claeson, G., Aurell, L., Karlsson, G., and Fiberger, P. (1977) In: New Methods for the Analysis of Coagulation Using Chromogenic Substrates (ed. by Witt, I.), pp. 251–259, Walter de Gruyter, Berlin, New York.
Glavin, S. A., Bobbitt, J. L., Shuman, R. T. and Smithwich, E. L. Jr. (1977). Use of peptidyl-4-methoxy-2-naphthylamides to assay plasmin. Anal. Biochem. 80, 355–365.
Davie, E. W., Rougie, C. and Lundblad, R. L. (1969) In: Recent Advances in Blood Coagulation (ed. by L. Poller), pp. 13–27, J. A. Churchill Hill Ltd., London.
Deutsch, D. G. and Mertz, E. T. (1970). Plasminogen: Purification from human plasma by affinity chromatography. Science, 170, 1095–1096.
Fujikawa, K., Legaz, M. E. and Davie, E. W. (1972). Bovine Factor X1 (Stuart factor). Mechanism of activation by a protein from Russell’s viper venom. Biochemistry, 11, 4892–4899.
Fujiwara, K. and Tsuru, D. (1978). New chromogenic and fluorogenic substrates for pyrorridonyl peptidase. J. Biochem. 83, 1145–1149.
Graf, L., Barat, E., Borvendeg, J., Hermann, J. and Patthy, A. (1976). Action of thrombin on ovine, bovine and human pituitary growth hormones. Eur. J. Biochem. 64, 333–340.
Han, Y. N., Kato, H., Iwanaga, S. and Komiya, M. (1978). Primary structure of bovine plasma high-molecular-weight kininogen, characterization of carbohydrate-free fragment 1.2 (fragment X) and its biological activity. J. Biochem. 83, 223–235.
Harada, T., Morita, T. and Iwanaga, S. (1978). A new assay method for bacterial endotoxins using horseshoe crab clotting enzyme. J. Med. Enz. (in Japanese), 3, 43–60.
Huseby, R. M., Clavin, S. A., Smith, R. E., Hull, R. N. and Smitheick, E. L. Jr. (1977). Studies on tissue culture plasminogen activator II. The detection and assay of urokinase and plasminogen activator from LLC-PK1 cultures (porcine) by the synthetic substrate Nd -benzyloxycarbonyl-glycyl-glycyl-arginyl-4-methoxy-2-naphthylamide. Thrombosis Research, 10, 679–687.
Iwanaga, S., Morita, T., Harada, T., Nakamura, S., Niwa, M., Takada, K., Kimura, T., and Sakakibara, S. (1978). Chromogenic substrates for horseshoe crab clotting enzyme. Its application for the assay of bacterial endotoxins. Haemostasis, 7, 183–188.
Kanaoka, Y., Takahashi, T. and Nakayama, H. (1977). A new fluoro-genic substrate for aminopeptidase. Chem. Pharm. Bull. 25, 362–363.
Katayama, K., Ericsson, L. H., Wade, R. D., Fujikawa, K., Walsh, K. A., Neurath, H. and Titani, K. (1978). Structural studies of bovine Factor IX. Fe. Proc. 37, 1617.
Kato, T., Nagatsu, T., Kimura, T. and Sakakibara, S. (1977). Seikagaku (in Japanese), 49, 990.
Kato, H., Adachi, N., Iwanaga, S., Abe, K., Takada, K., Kimura, T. and Sakakibara, S. (1978) In: Abstract, New assay method for kallikrein in urine, using fluorogenic peptide substrate. The 98th Congress on Pharmaceutical Society of Japan held in Okayama on April 5 to 9, p. 485.
Magnusson, S., Sottrup-Jensen, L. and Petersen, T. E. (1975) In: Prothrombin and Related Coagulation Factors (ed by Hemker, H. C. Veltkamp, J. J.) pp. 25–46, Leiden University Press, Leiden.
Mikuni, Y., Iwanaga, S. and Konishi, K. (1973). A peptide released from plasma fibrin stabilizing factor in the conversion to the active enzyme by thrombin. Biochem. Biophys. Res. Communs. 54, 1393–1402.
Morita, T., Iwanaga, S. and Suzuki, T. (1974). Studies on the activation of bovine prothrombin. Isolation and characterization of the fragments released from the prothrombin by activated factor Xa. J. Biochem. 76, 1031–1048.
Morita, T. and Iwanaga, S. (1978). Purification and properties of prothrombin activator from the venom of Echis carinatus. J. Biochem. 83, 559–570.
Nakabayashi, M., Chin, N., Ogino, M., Kaneko, Y., Sato, K. and Sakamoto, M. (1978) In: Abstract (in Japanese), The 1st Congress of Japanese Society on Thrombosis and Hemostasis. p. 60.
Nakamura, S., Iwanaga, S., Suzuki, T., Mikuni, Y. and Konishi, K. (1974). Amino acid sequence of the peptide released from bovine factor XIII following activation by thrombin. Biochem. Biophys. Res. Communs. 58, 250–256.
Nakamura, S., Morita, T., Iwanaga, S., Niwa, M. and Takahashi, K. (1977) Seikagaku (in Japanese) 49, 759.
Nakamura, S., Morita, T., Iwanaga, S., Niwa, M. and Takahashi, K. (1977). A sensitive substrate for the clotting enzyme in horseshoe crab hemocytes. J. Biochem. 81, 1567–1569.
Nieuwenhuizen, W., Wijngaads, G. and Groeneveld, E. (1977). genic peptide amide substrates for the estimation of plasminogen activators and plasmin. Anal. Biochem. 83, 143–148.
Ogawa, N., Yamamoto, H., Katamine, T. and Tajima, H. fication and some properties of urokinase. Haemorrh. (Stuttg.), 34, 194–209.
Ottesen, M. (1967). Induction of biological activity by limited proteolysis. Ann. Rev. Biochem. 36, 55–76.
Sugo, T., Kato, H., Iwanaga, S., and Fujii, S. (1978). Seikagaku (in Japanese) 50, 763.
Svendsen, L., BlombHck, B., BlombHck, M. and Olsson, P. (1972). Synthetic chromogenic substrates for determination of trypsin, thrombin, and thrombin-like enzymes. Thrombosis Research, 1, 267–278.
Takahashi, H., Nagasawa, S. and Suzuki, T. (1972). Studies on prekallikrein of bovine plasma. I. Purification and properties. J. Biochem. 71, 471–483.
Wiman, B. (1973). Primary structure of peptides released during activation of human plasminogen by urokinase. Eur. J. Biochem. 39, 1–9.
Zimmerman, M., Yurewicz, E. C. and Patel, G. (1976). A new fluoro-genic substrate for chymotrypsin. Anal. Biochem. 70, 258–262.
Zimmerman, M., Ashe, B., Yurewicz, E. C. and Patel, G. (1977). Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates. Anal. Biochem. 78, 47–51.
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Iwanaga, S. et al. (1979). Fluorogenic Peptide Substrates for Proteases in Blood Coagulation, Kallikrein-Kinin and Fibrinolysis Systems. In: Fujii, S., Moriya, H., Suzuki, T. (eds) Kinins—II. Advances in Experimental Medicine and Biology, vol 120. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0926-1_15
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