Linked Life Data

6460619

Source:http://linkedlifedata.com/resource/pubmed/id/6460619

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-5-21
pubmed:abstractText
The 2'(3')-O-trinitrophenyl (N3ph) derivatives of the adenine nucleotides are strong competitive inhibitors of isolated mitochondrial ATPase (factor F1). Ki decreases in the order N3phAdo greater than N3phAdo greater than N3phAMP greater than N3phADP and is equal to 8 nM for N3phADP. Picric acid, which activates the ATPase reaction of factor F1 without changing the Km(app), prevents the inhibiting action of N3phADP. At pH 7.6 the inhibiton of factor F1 is accompanied by the binding of one molecule of N3phADP to a molecule of the enzyme. This binding leads to changes in the absorption spectrum, but not in the intensity of the fluorescence of the N3phADP. At pH 6.7 one or two molecules of N3phADP bind with the tight binding sites of factor F1. This binding is accompanied by the manifold enhancement of the fluorescence of N3phADP. The results obtained indicate that the sites of factor F1 that tightly bind nucleotides are immersed in the hydrophobic pocket of the protein molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
121
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
451-5
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Using 2'(3')-O-trinitrophenyl derivatives of adenine nucleotides to study the structure and mechanism of functioning of soluble mitochondrial ATPase.
pubmed:publicationType
Journal Article