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. 1984 Dec;76(4):1065–1069. doi: 10.1104/pp.76.4.1065

Purification and Properties of the Constitutive Arginase of Evernia prunastri1

Angeles Martín-Falquina 1, María Estrella Legaz 1
PMCID: PMC1064435  PMID: 16663950

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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