Plant Physiol.
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Plant Physiology 76:1065-1069 (1984)
© 1984 American Society of Plant Biologists

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Articles

Purification and Properties of the Constitutive Arginase of Evernia prunastri1

Angeles Martín-Falquina and María Estrella Legaz

Department of Plant Physiology, The Lichen Team, Faculty of Biology, Complutense University, 28040 Madrid, Spain

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.

1 Supported by grant No. 0365 C02-02 from the CAICYT (Spain).






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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1984 by the American Society of Plant Biologists