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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
|
| pubmed:dateCreated |
1989-1-26
|
| pubmed:abstractText |
1. The inhibition of F1-ATPase by its natural peptide inhibitor is mixed non-competitive with two pH optimum values (5.5 and 8.2). 2. A two-step model for the interaction is suggested in which two enzyme conformations would exhibit different affinities for the peptide. 3. At low pH, interaction would be favoured. At high pH, a conformation (not susceptible to inhibition) changes into another (susceptible to inhibition) through the hydrolytic reaction stimulation, due to high pH.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0020-711X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
20
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
977-81
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2904383-Animals,
pubmed-meshheading:2904383-Cattle,
pubmed-meshheading:2904383-Hydrogen-Ion Concentration,
pubmed-meshheading:2904383-Kinetics,
pubmed-meshheading:2904383-Mitochondria, Liver,
pubmed-meshheading:2904383-Proteins,
pubmed-meshheading:2904383-Proton-Translocating ATPases,
pubmed-meshheading:2904383-Rats
|
| pubmed:year |
1988
|
| pubmed:articleTitle |
Interaction of F1-ATPase and its inhibitor peptide. Effect of pH.
|
| pubmed:affiliation |
Department of Biochemistry, University of Navarra, Pamplona, Spain.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|