Purification and Properties of the Constitutive Arginase of Evernia prunastri
Open Access
- 1 December 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 76 (4) , 1065-1069
- https://doi.org/10.1104/pp.76.4.1065
Abstract
Constitutive arginase (molecular weight 330,000) 920-fold purified from Evernia prunastri thallus, is activated by putrescine, l-ornithine, and agmatine with Ka values of 2.7, 1.1, and 5.8 millimolar, respectively. Constitutive arginase is also activated by endogenous l-arginine, reaching its maximum activity at 16 hours of incubation on Tris-HCl (pH 9.15) with a subsequent decrease. Urea behaves as a mixed inhibitor of the enzyme with a Ki value of 2.6 millimolar. Atranorin and evernic acid behave as in vitro activators of the enzyme; usnic acid does not have any significant effect as activator.This publication has 14 references indexed in Scilit:
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