Linked Life Data

2857551

Source:http://linkedlifedata.com/resource/pubmed/id/2857551

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-3-21
pubmed:abstractText
This study examined the inhibition of azide as a probe of the magnesium regulation of beef heart mitochondrial ATPase (F1) catalysis. Azide elicited a slow hysteretic effect on both ATP and ITP hydrolysis of F1. This hysteretic effect was shown to be due to the consecutive binding of magnesium and azide, and to be independent of catalytic turnover. The azide binding site was also shown to be separate from the anion binding HCO3- site on F1. The results presented indicate that metal binding is important in the inhibition of the hydrolytic activity and regulation of F1. A model is presented which is consistent with the hysteretic inhibition of F1 by azide, in which there is a slow equilibration between free enzyme and the enzyme-magnesium-azide complex.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
236
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
815-24
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Interaction of azide with beef heart mitochondrial ATPase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.