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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1984-10-25
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pubmed:abstractText |
The 'high ammonia pathway' enzyme glutamate dehydrogenase (NADP+) is inactivated in cells of Pseudomonas aeruginosa when the stationary phase of growth is reached. Purified glutamate dehydrogenase (NADP+) appeared to be a protein composed of six identical subunits with a molecular weight of 54 000. With antibodies raised against purified enzyme it was found that glutamate dehydrogenase (NADP+) inactivation is accompanied by a parallel decrease in immunologically reactive material. This suggests that glutamate dehydrogenase (NADP+) inactivation is caused or followed by rapid proteolysis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
801
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32-9
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pubmed:dateRevised |
2000-12-18
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pubmed:meshHeading |
pubmed-meshheading:6432059-Antigen-Antibody Complex,
pubmed-meshheading:6432059-Cross Reactions,
pubmed-meshheading:6432059-Glutamate Dehydrogenase,
pubmed-meshheading:6432059-Immune Sera,
pubmed-meshheading:6432059-Immunodiffusion,
pubmed-meshheading:6432059-Kinetics,
pubmed-meshheading:6432059-NADP,
pubmed-meshheading:6432059-Pseudomonas aeruginosa
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pubmed:year |
1984
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pubmed:articleTitle |
Purification of NADP-dependent glutamate dehydrogenase from Pseudomonas aeruginosa and immunochemical characterization of its in vivo inactivation.
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pubmed:publicationType |
Journal Article
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