Linked Life Data

1534982

Source:http://linkedlifedata.com/resource/pubmed/id/1534982

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-7-14
pubmed:abstractText
A membrane-bound ATPase from the archaebacterium Halobacterium saccharovorum is inhibited by N-ethylmaleimide in a nucleotide-protectable manner (Stan-Lotter et al., 1991, Arch. Biochem. Biophys. 284, 116-119). When the enzyme was incubated with N-[14C]ethylmaleimide, the bulk of radioactivity was associated with the 87,000-Da subunit (subunit I). ATP, ADP, or AMP reduced incorporation of the inhibitor. No charge shift of subunit I was detected following labeling with N-ethylmaleimide, indicating an electroneutral reaction. The results are consistent with the selective modification of sulfhydryl groups in subunit I at or near the catalytic site and are further evidence of a resemblance between this archaebacterial ATPase and the vacuolar-type ATPases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
296
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
347-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Nucleotide-protectable labeling of sulfhydryl groups in subunit I of the ATPase from Halobacterium saccharovorum.
pubmed:affiliation
Institut für Mikrobiologie und Genetik, Universität Wien, Vienna, Austria.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't