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NEW SUBSTRATES OF TRYPSIN AND SOME TRYPSIN-LIKE ENZYMES

G. G. GLENNER 1, V. K. HOPSU 1, and L. A. COHEN 1

1 Laboratory of Experimental Pathology and Laboratory of Chemistry, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland

The results of the investigation of two new naphthyl substrates of trypsin and the trypsinlike enzyme(s) in human mast cells, carbobenzyloxy-l-arginine and benzoyl-l-arginine beta-naphthylamide, have led directly to the synthesis and study of a further substrate, carbobenzyloxy-l-arginine methyl ester. The activity of trypsin against the carbobenzyloxy ester is greater than that previously described biochemically for other synthetic substrates. The inhibition of the amidase and esterase activity of trypsin and the tryptic enzyme in human mast cells by egr-aminocaproic acid derivatives is characterized and evidence is presented to show that this enzymic activity in human mast cells is more closely related to trypsin than to plasmin (fibrinolysin).

Submitted on February 3, 1964


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