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Downum KR, Rosenthal GA, Cohen WS. l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. Plant Physiol. 1983;73(4):965-8doi: 10.1104/pp.73.4.965.
Downum, K. R., Rosenthal, G. A., & Cohen, W. S. (1983). l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. Plant physiology, 73(4), 965-8. https://doi.org/10.1104/pp.73.4.965
Downum, K R, et al. "l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr." Plant physiology vol. 73,4 (1983): 965-8. doi: https://doi.org/10.1104/pp.73.4.965
Downum KR, Rosenthal GA, Cohen WS. l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr. Plant Physiol. 1983 Dec;73(4):965-8. doi: 10.1104/pp.73.4.965. PMID: 16663352; PMCID: PMC1066589.
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Plant Physiol. 1983 Dec;73(4):965-8. doi: 10.1104/pp.73.4.965.

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

Plant physiology

K R Downum, G A Rosenthal, W S Cohen

Affiliations

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

PMID: 16663352 PMCID: PMC1066589 DOI: 10.1104/pp.73.4.965

Abstract

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.

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