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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1983-6-17
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pubmed:abstractText |
Isolated oligomycin-sensitive ATPase undergoes a kinetic change at 20-25 degrees C with a higher activation energy and a lower Km for ATP below this temperature range. This observation has been correlated with temperature-dependent structural changes detected by circular dichroism in the UV region in the isolated enzyme. The negative ellipticities in the 208-225 nm region, which are proportional to the alpha-helix content, increase with rise in temperature to a maximum above 25 degrees C.
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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 |
May
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
|
pubmed:volume |
155
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6220922-Adenosine Triphosphatases,
pubmed-meshheading:6220922-Animals,
pubmed-meshheading:6220922-Cattle,
pubmed-meshheading:6220922-Circular Dichroism,
pubmed-meshheading:6220922-Kinetics,
pubmed-meshheading:6220922-Mitochondria, Heart,
pubmed-meshheading:6220922-Oligomycins,
pubmed-meshheading:6220922-Protein Conformation,
pubmed-meshheading:6220922-Temperature
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pubmed:year |
1983
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pubmed:articleTitle |
Temperature-dependent conformational changes in isolated oligomycin-sensitive ATPase.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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