Source:http://linkedlifedata.com/resource/pubmed/id/16663352
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2010-6-29
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| pubmed:abstractText |
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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| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-1257764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-12999819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-16657449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-16659111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-16660151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-16660904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-16747276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-4765636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-7140765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-7306133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16663352-942051
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0032-0889
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
73
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
965-8
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| pubmed:dateRevised |
2010-9-15
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| pubmed:year |
1983
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| pubmed:articleTitle |
l-Arginine and l-Canavanine Metabolism in Jack Bean, Canavalia ensiformis (L.) DC. and Soybean, Glycine max (L.) Merr.
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| pubmed:affiliation |
T. H. Morgan School of Biological Sciences, University of Kentucky, Lexington, Kentucky 40506.
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| pubmed:publicationType |
Journal Article
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