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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-6-29
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pubmed:abstractText |
We have employed the driven 31P-NMR saturation transfer method to measure in vivo the temperature dependence of the forward and reverse unidirectional fluxes of the arginine kinase reaction in the tail muscle of a live shrimp, Sycionia ingentis. Our results indicated that neither the forward nor the reverse rate constants of this reaction were significantly temperature-dependent between 8 and 16 degrees C, in contrast to the kinetic characteristics of isolated arginine kinases.
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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 |
Apr
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
1135
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1591272-Adenosine Triphosphate,
pubmed-meshheading:1591272-Animals,
pubmed-meshheading:1591272-Arginine Kinase,
pubmed-meshheading:1591272-Crustacea,
pubmed-meshheading:1591272-Kinetics,
pubmed-meshheading:1591272-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1591272-Models, Theoretical,
pubmed-meshheading:1591272-Muscles,
pubmed-meshheading:1591272-Phosphorus,
pubmed-meshheading:1591272-Temperature
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pubmed:year |
1992
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pubmed:articleTitle |
Temperature dependence of arginine kinase reaction in the tail muscle of live Sycionia ingentis as measured in vivo by 31P-NMR driven saturation transfer.
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pubmed:affiliation |
Department of Land, Air and Water Resources, University of California, Davis 95616.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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