A thiol protease of peritoneal macrophages in the guinea pig.
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.
D000818:Animals; D001202:Ascitic Fluid / Q000473:pathology; D002851:Chromatography, High Pressure Liquid; D003374:Coumarins / Q000378:metabolism; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D005260:Female; D006168:Guinea Pigs; D006863:Hydrogen-Ion Concentration; D008264:Macrophages / Q000201:enzymology*; D008297:Male; D008970:Molecular Weight; D009842:Oligopeptides / Q000378:metabolism; D011480:Protease Inhibitors; D013379:Substrate Specificity
D003374:Coumarins; D009842:Oligopeptides; D011480:Protease Inhibitors; C048055:tertiary-butyloxycarbonyl-phenylalanyl-seryl-arginyl-4-methylcoumarin-7-amide; D010450:Endopeptidases; D003546:Cysteine Endopeptidases