Experientia. Basel 1986-02-15

A thiol protease of peritoneal macrophages in the guinea pig.

T Kambara, S Uchida, J Tanaka, S Shoji

Index: Experientia 42(2) , 155-7, (1986)

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Abstract

Proteolytic enzymes of the guinea pig peritoneal exudate macrophages were investigated using synthetic fluorogenic peptide substrates. Among several enzymes, t-butyloxycarbonyl-phenylalanyl-seryl-arginine 4-methylcoumaryl-7-amide cleaving enzymes had the highest activity, and the activity in exudate macrophages was about 3 times stronger than that in resident macrophages. The molecular weight of the enzyme was around 35,000 and optimal pH around 6.5-7.0. It was inhibited by thiol-blocking reagents, suggesting a thiol protease.

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Boc-Phe-Ser-Arg-AMC Structure Boc-Phe-Ser-Arg-AMC
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