Proteolytic enzymes in green wheat-leaves III. Inactivation of acid proteinase II by diazoacetyl-DL-norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)-propane
- 1 August 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 19 (5), 819-824
- https://doi.org/10.1093/oxfordjournals.pcp.a075656
Abstract
Acid proteinase II isolated from green wheat leaves in a purified form was rapidly inactivated at pH=5.5 to 6.0 by a 50-fold molar excess of diazoacetyl-DL-norleucine methyl ester (DAN) in the presence of cupric ions which were essential for inactivation. The acid proteinase was also inactivated by reaction with 1,2-epoxy-3-(p-nitrophenoxy)-propane (EPNP). The inactivation by EPNP was much slower than by DAN and the half-life of the activity was 24 hr.Keywords
This publication has 2 references indexed in Scilit:
- The Structure and Function of Acid Proteases. VI. Effects of Acid Protease-Specific Inhibitors on the Acid Proteases from Aspergillus niger var. macrosporus1The Journal of Biochemistry, 1976
- The Inactivation of Pepsin by Diazoacetylnorleucine Methyl EsterJournal of Biological Chemistry, 1966