Linked Life Data

7642655

Source:http://linkedlifedata.com/resource/pubmed/id/7642655

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
1995-9-18
pubmed:abstractText
The plasma membrane proton pump (H(+)-ATPase) of yeast energizes solute uptake by secondary transporters and regulates cytoplasmic pH. The addition of glucose to yeast cells stimulates proton efflux mediated by the H(+)- ATPase. A > 50-fold increase in proton extrusion from yeast cells is observed in vivo, whereas the ATPase activity of purified plasma membranes is increased maximally 8-fold after glucose treatment (Serrano, R. (1983) FEBS Lett. 156, 11-14). The low capacity of yeast cells for proton extrusion in the absence of glucose can be explained by the finding that, in H(+)-ATPase isolated from glucose-starved cells, ATP hydrolysis is essentially uncoupled from proton pumping. The number of protons transported per ATP hydrolyzed is significantly increased after glucose activation. We suggest that intrinsic uncoupling is an important mechanism for regulation of pump activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
270
pubmed:geneSymbol
PMA1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19659-67
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Metabolic modulation of transport coupling ratio in yeast plasma membrane H(+)-ATPase.
pubmed:affiliation
Department of Plant Biology, Royal Veterinary and Agricultural University, Frederiksberg, Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't