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Articles

L-Arginine and L-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. ¹

T. H. Morgan School of Biological Sciences, University of Kentucky, Lexington, Kentucky 40506

Studies have been conducted with the arginase (L-arginine amidinohydrolase, EC 3.5.3.1) of two legumes: jack bean, Canavalia ensiformis (L.) DC., a L-canavanine-containing plant and soybean, Glycine max, a canavanine-free species. Analyses of the arginase obtained from gradient-purified mitochondria of these legumes revealed that the arginine-dependent (ADA) and canavanine-dependent activities (CDA) were localized within this organelle.

Kinetic analyses of affinity-purified mitochondrial arginase revealed an apparent K_m of 7 to 8 millimolar for arginine with both the jack bean and soybean arginases. Comparable determinations with canavanine revealed an apparent K_m of 38 millimolar with the jack bean enzyme; the affinity for this arginine analog with the soybean enzyme is so poor that product formation remained linear even with a canavanine concentration of 890 millimolar.

A single macromolecule appears to be responsible for both the ADA and CDA of jack bean arginase. Ion-exchange chromatography of mitochondrial arginase revealed that the ADA and CDA eluted as a single, discrete peak from DEAE-cellulose. Analyses with arginine- and canavanine-linked Sepharose failed to reveal more than one enzyme. Both the ADA and CDA increased by nearly identical amounts following elution from arginine- and canavanine-linked cyanogen bromide-activated sepharose. Neither ADA nor CDA increased preferentially over the other.

¹ Supported by the National Science Foundation (PCM-78-20167) United States Department of Agriculture/Science and Education Administration/Competitive Research Grants Organization (59-2211-0-1-495-0). National Institutes of Health (AM-17322), and the Research Committee of the University of Kentucky.