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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7-8
|
| pubmed:dateCreated |
1978-6-12
|
| pubmed:abstractText |
Binding of MgATP to yeast phosphofructokinase was investigated by the gel filtration equilibrium dialysis technique. Per subunit of yeast phosphofructokinase two molecules of MgATP are bound in the absence of fructose-6-phosphate, one to a high-affinity and one to a low-affinity site. The experimental data were compared with a kinetic model of yeast phosphofructokinase as described by Freyer et al. [3].
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0001-5318
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
36
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1027-33
|
| pubmed:dateRevised |
2001-11-2
|
| pubmed:meshHeading |
pubmed-meshheading:148197-Adenosine Triphosphate,
pubmed-meshheading:148197-Binding Sites,
pubmed-meshheading:148197-Catalysis,
pubmed-meshheading:148197-Magnesium,
pubmed-meshheading:148197-Molecular Weight,
pubmed-meshheading:148197-Phosphofructokinase-1,
pubmed-meshheading:148197-Saccharomyces cerevisiae
|
| pubmed:year |
1977
|
| pubmed:articleTitle |
Binding of MgATP to yeast phosphofructokinase.
|
| pubmed:publicationType |
Journal Article
|