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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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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DOI: https://doi.org/10.1007/978-1-4757-0926-1_15
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