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- W2317962532 startingPage "4060" @default.
- W2317962532 abstract "Various peptide anilides were synthesized by a conventional method with the object of obtaining specific substrates for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE) in order to compare the substrate specificity of SFP with that of LE. It was found that the P1 Val compound among succinyl tripeptide p-nitroanilides (Suc-Tyr-Leu-X-pNA) exhibited the highest kcat/Km values for hydrolysis by SFP and LE, however, the tetrapeptide Suc-Ala-Tyr-Leu-Val-pNA [kcat/Km values (M-1S-1) for hydrolysis by SFP and LE : 84000 and 48000, respectively] was the preferred chromogenic substrate for SFP and LE because of its high solubility in the buffer and its moderate kcat/Km values. The substrate specificity of SFP was found to be similar to that of LE." @default.
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- W2317962532 date "1982-01-01" @default.
- W2317962532 modified "2023-10-16" @default.
- W2317962532 title "Synthesis of chromogenic substrates specific for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE)." @default.
- W2317962532 cites W1768927099 @default.
- W2317962532 doi "https://doi.org/10.1248/cpb.30.4060" @default.
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