Linked Life Data

3024745

Source:http://linkedlifedata.com/resource/pubmed/id/3024745

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1987-2-19
pubmed:abstractText
Gastric acid secretion results from the activity of a specific ATPase, the (H+,K+)-ATPase. This enzyme, discovered in 1973, exchanges H+ for K+. It has two ATP binding sites, both involved in enzyme activity, whose affinities vary as a function of the H+ and K+ concentrations. Hydrolysis of ATP at the highest affinity site leads to the synthesis of a covalent aspartyl phosphate which accumulates in the absence of K+. The presence of this cation accelerates dephosphorylation resulting in the stimulation of ATPase (and PNPPase) activity. The structure of membranous (H+,K+)-ATPase is poorly defined. n-Octylglucoside solubilizes an active enzyme of 390-420 kDa which can be partly depolymerized using cholate. The monomer, characterized in SDS has a 95 kDa molecular mass and is inactive. In the presence of magnesium, (H+,K+)-ATPase catalyzes the active and neutral exchange of H+ for K+ at the expense of ATP. In the absence of ATP, (H+,K+)-ATPase acts as a passive transporter exchanging K+ for K+ at maximal rate and H+ for K+ at a 20 times slower rate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1287-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Gastric (H+,K+)-ATPase.
pubmed:publicationType
Journal Article