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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1977-11-25
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pubmed:abstractText |
The protective effect of ATP, ADP and GTP against the inactivation of Ca2+ + Mg2+ -dependent ATPase by the thiol reagent NBD-chloride is used to calculate the apparent dissociation constants (K'D) of nucleotide enzyme complexes on the basis of a simple kinetic model. The K'D-values of the complexes with Mg-ATP (80 micrometer) and Mg-GTP (500 micrometer) are found to be rather close to their Km-values in the high concentration range supporting maximum activity. The requirement of the occupancy of the low affinity site by Mg ATP for a high rate of the Ca2+ transport system is explained in terms of the flip-flop mechanism established earlier for the analogous Na+ + K+-transporting ATPase system.
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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:issn |
0001-5318
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
K1-10
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:143860-4-Chloro-7-nitrobenzofurazan,
pubmed-meshheading:143860-Adenosine Triphosphatases,
pubmed-meshheading:143860-Animals,
pubmed-meshheading:143860-Binding Sites,
pubmed-meshheading:143860-Calcium,
pubmed-meshheading:143860-Dissociative Disorders,
pubmed-meshheading:143860-Enzyme Repression,
pubmed-meshheading:143860-Humans,
pubmed-meshheading:143860-Magnesium,
pubmed-meshheading:143860-Rabbits,
pubmed-meshheading:143860-Sarcoplasmic Reticulum
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pubmed:year |
1977
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pubmed:articleTitle |
Determination and functional significance of low affinity nucleotide sites of Ca2+ + Mg2+ -dependent ATPase of sarcoplasmic reticulum.
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pubmed:publicationType |
Journal Article
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