Cytochemical demonstrations of protease in human peripheral blood cells by use of new alpha-naphthyl ester substrates.
The proteases of human leukocytes were cytochemically studied by use of new alpha-naphthyl esters, tosyl-L-lysine-alpha-naphthyl ester (TLNE) and acetyl-L-tyrosine-alpha-naphthyl ester (ATNE). The hydrolytic activities were strong only in neutrophils, with both substrates. They were inhibited completely by DFP and chymostatin, but not by leupeptin and iodoacetate. These results indicate that chymotrypsin-like enzyme(s), capable of hydrolyzing both substrates, exist in neutrophils.
D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D006651:Histocytochemistry; D006801:Humans; D007461:Iodoacetates / Q000494:pharmacology; D019807:Iodoacetic Acid; D007531:Isoflurophate / Q000494:pharmacology; D007962:Leukocytes / Q000201:enzymology*; D007976:Leupeptins / Q000494:pharmacology; D008239:Lysine / Q000031:analogs & derivatives; D008297:Male; D009284:Naphthols; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology; D009842:Oligopeptides / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000032:analysis*; D011480:Protease Inhibitors; D013379:Substrate Specificity; D014443:Tyrosine / Q000031:analogs & derivatives
D007461:Iodoacetates; D007976:Leupeptins; D009284:Naphthols; D009842:Oligopeptides; D011480:Protease Inhibitors; C031968:tosyllysine alpha-naphthyl ester; D007531:Isoflurophate; D014443:Tyrosine; C038260:N-acetyltyrosine 1-naphthyl ester; C002101:chymostatin; C029204:alpha-naphthyl butyrate; D010447:Peptide Hydrolases; D002918:Chymotrypsin; C032854:leupeptin; D008239:Lysine; D019807:Iodoacetic Acid