NEW SUBSTRATES OF TRYPSIN AND SOME TRYPSIN-LIKE ENZYMES
Open Access
- 1 July 1964
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 12 (7), 545-551
- https://doi.org/10.1177/12.7.545
Abstract
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 β-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 ε-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).Keywords
This publication has 2 references indexed in Scilit:
- FURTHER OBSERVATIONS ON HISTOCHEMICAL ESTERASE AND AMIDASE ACTIVITIES WITH SIMILARITIES TO TRYPSINJournal of Histochemistry & Cytochemistry, 1963
- Antifibrinolytic Activity of Certain PectinsThrombosis and Haemostasis, 1961