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An insoluble spleen fibrinolytic serine proteinase(SFP) extracted from the human spleen with 2 M NaClO4 and partially purified by the authors was characterized with its enzymatic capability to split fibrin and fibrinogen at neutral pH. Its substrate specificity was much limited; any synthetic peptide substrates for factors of coagulation and fibrinolysis were not hydrolyzed. The present studies were therefore made to search for SFP peptide substrate which mimicked possible natural substrates, using the partially purified enzyme preparation showing single protein band possessing fibrinolytic activity on polyacrylamide gel disk electrophoresis.  Despite of fact that various chromogenic peptide substrates having principal structure of -Arg-pNA and -Lys-pNA and various esters of Lys, Arg, Try, Phe and Tyr were not decomposed by SFP, a clue was however found that Suc-Ala-Ala-Ala-pNA (substrate for elastase) was decomposed by SFP but very slowly. Then, trial to mimic a part of insulin B chain (a substrate for elastase) led us to reach Suc-Tyr-Leu-Val-pNA which was well amidolyzed by SFP with Km of 0.17 mM and Kcat/Km(M) of 22,600. Further, Suc-Ala- Tyr-Leu-Val-pNA was found more appropriate substrate than the former. It was noteworthy that ratio of SFP susceptibility of Suc-Ala-Pro-Val-pNA, Suc-Ala-Pro-Ala-pNA and Suc-Ala-Pro-Leu-pNA was approximately 9:1:0.  Results obtained sofar concluded that synthetic peptide substrates appropriate for SFP are dominantly characterized by the C-terminal-Val; other part amino acid sequences is also significant however.

New Synthetic Peptide Substrates Of -Val-pNA Type For An Insoluble Fibrinolytic Serine Enzyme Extracted From Human Spleen