Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1989-8-3
|
pubmed:abstractText |
Mitochondrial F1 containing genetically modified beta-subunit was purified for the first time from a mutant of the yeast Schizosaccharomyces pombe. Precipitation by poly(ethylene glycol) allowed us to obtain a very stable and pure enzyme from either mutant or wild-type strain. In the presence of EDTA, purified F1 retained high amounts of endogenous nucleotides: 4.6 mol/mol and 3.7 mol/mol for mutant and wild-type F1, respectively. The additional nucleotide in mutant F1 was ATP; it was lost in the presence of Mg2+, which led to a total of 3.4 mol of nucleotides/mol whereas wild-type F1 retained all its nucleotides. Mutant F1 bound more exogenous ADP than wild-type F1 and the same total nucleotide amount was reached with both enzymes. Kinetics of ATPase activity revealed a much higher negative cooperativity for mutant than for wild-type F1. Bicarbonate abolished this negative cooperativity, but higher concentrations were required for mutant F1. The mutant enzyme was more sensitive than the wild-type one to azide inhibition and ADP competitive inhibition; this indicated stronger interactions between nucleotide and F1 in the mutant enzyme. The latter also showed increased sensitivity to N,N'-dicyclohexylcarbodiimide irreversible inhibition.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
23
|
pubmed:volume |
975
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
119-26
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2525405-Adenosine Diphosphate,
pubmed-meshheading:2525405-Adenosine Triphosphate,
pubmed-meshheading:2525405-Chromatography, Gel,
pubmed-meshheading:2525405-Kinetics,
pubmed-meshheading:2525405-Macromolecular Substances,
pubmed-meshheading:2525405-Magnesium,
pubmed-meshheading:2525405-Mutation,
pubmed-meshheading:2525405-Protein Binding,
pubmed-meshheading:2525405-Proton-Translocating ATPases,
pubmed-meshheading:2525405-Saccharomycetales,
pubmed-meshheading:2525405-Schizosaccharomyces,
pubmed-meshheading:2525405-Submitochondrial Particles
|
pubmed:year |
1989
|
pubmed:articleTitle |
Purification from a yeast mutant of mitochondrial F1 with modified beta-subunit. High affinity for nucleotides and high negative cooperativity of ATPase activity.
|
pubmed:affiliation |
Laboratoire de Biologie et Technologie des Membranes du CNRS, Université Claude Bernard de Lyon, Villeurbanne, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|