CARBOXYPEPTIDASE A: APPROACHES TO THE CHEMICAL NATURE OF THE ACTIVE CENTER AND THE MECHANISMS OF ACTION
- 1 January 1963
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 49 (1) , 109-116
- https://doi.org/10.1073/pnas.49.1.109
Abstract
Acylatlon with monocarboxylic acid anhydride iodometric photooxidation of carboxy-peptidase, or the replacement of the zinc of carboxypeptidase by cadmium or mercury all increase esterase and decrease peptidase activities of this enzyme. The pH-rate profiles of peptidase and esterase activities differ significantly. These data, in conjunction with studies indentifying the groups of the substrate essential for the formation of enzyme complexes, lead to suggestions concerning the distinctive mechansims of peptidase and esterase action respectively.Keywords
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