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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1989-7-5
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pubmed:abstractText |
1. The binding kinetics for [35S]thiamine pyrophosphate to transketolase and the dependency of transketolase on divalent cations for activity were investigated. 2. With Scatchard analysis, dissociation constant (Kd) and n value were calculated to be 0.2 x 10(-6) M and 0.66 respectively. 3. The activity of the reconstituted enzyme increased in the order of Co2+ less than Mn2+ less than Ca2+ less than Mg2+. The native transketolase contained Mg2+ in its molecular structure.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0020-711X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1255-9
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:3248678-Binding Sites,
pubmed-meshheading:3248678-Calcium,
pubmed-meshheading:3248678-Catalysis,
pubmed-meshheading:3248678-Enzyme Activation,
pubmed-meshheading:3248678-Erythrocytes,
pubmed-meshheading:3248678-Humans,
pubmed-meshheading:3248678-Hydrogen-Ion Concentration,
pubmed-meshheading:3248678-Magnesium,
pubmed-meshheading:3248678-Manganese,
pubmed-meshheading:3248678-Thiamine Pyrophosphate,
pubmed-meshheading:3248678-Transketolase
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pubmed:year |
1988
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pubmed:articleTitle |
Studies on the nature of thiamine pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes.
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pubmed:affiliation |
Department of Hygiene, Faculty of Medicine, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article
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