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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
1976-6-2
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pubmed:abstractText |
The complex formation between the ATP-analogous reactive dye Cibacron blue F3G-A and yeast phosphofructokinase is accompanied by a red shift of the visible absorption spectrum. From the position of lambdamax of the dye-phosphofructokinase complex in the polarity scales obtained from model solvents it may be concluded that the chromophoric system is evidently located in a highly apolaric range of the enzyme protein. The spectrophotometric titration of yeast phosphofructokinase with Cibacron blue F3G-A yielded a sigmoidal binding curve, which can be described by the MONOD-WYMAN-CHANGEUX model.
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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
|
pubmed:issn |
0001-5318
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1447-51
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pubmed:dateRevised |
2001-11-2
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pubmed:meshHeading | |
pubmed:year |
1975
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pubmed:articleTitle |
Specific binding of Cibacron blue F3G-A to yeast phosphofructokinase.
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pubmed:publicationType |
Journal Article
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