Carboxypeptidase in Mammalian Tissue.
- 1 May 1953
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 83 (1) , 10-14
- https://doi.org/10.3181/00379727-83-20249
Abstract
Using chloracetyl-L-tyrosine as substrate, carboxypeptidase was found widely distr. through mammalian tissues. Previous failures to detect the enzyme are due to: (a) the existence of a natural cellular inhibitor, which masks the enzyme; and (b)the enzyme probably exists in 2 forms. The pH optima of these 2 forms are different, and one is activated, the other inhibited, by cysteine. The natural inhibitor is protein in nature, affects only one of the forms and in a non- competitive fashion. The enzymatic conversion of one form of the enzyme to the other was detected in vitro.Keywords
This publication has 2 references indexed in Scilit:
- THE CHEMICAL NATURE AND MODE OF ACTION OF PANCREATIC CARBOXYPEPTIDASEJournal of Biological Chemistry, 1949
- Crystalline CarboxypolypeptidaseScience, 1935