Linked Life Data

16666844

Source:http://linkedlifedata.com/resource/pubmed/id/16666844

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-6-29
pubmed:abstractText
Lysophosphatidylcholine at concentrations of 30 micromolar stimulated the rate of MgATP-dependent H(+)-accumulation in oat (Avena sativa L. cv Rhiannon) root plasma membrane vesicles about 85% while the passive permeability of H(+) was unchanged. Activation was dependent on chain length, degree of saturation, and head group of the lysophospholipid. A H(+)-ATPase assay was developed that allowed the simultaneous measurement of proton pumping and ATPase activity in the same sample. ATP hydrolysis was also stimulated by lysophospholipids and showed the same lipid specificity, but stimulation was only about 25% at 30 micromolar. At higher concentrations of lysophosphatidylcholine the ATPase activity in a latency-free system could be stimulated about 150%. The enzymic properties of proton pumping and ATP hydrolysis were otherwise identical with respect to vanadate sensitivity, K(m) for ATP and pH optimum. The stimulatory effect of lysophospholipids suggests that these compounds could be part of the regulatory system for plant plasma membrane H(+)-ATPase activity in vivo.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jul
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1009-14
pubmed:dateRevised
2010-9-14
pubmed:year
1989
pubmed:articleTitle
Lysophosphatidylcholine stimulates ATP dependent proton accumulation in isolated oat root plasma membrane vesicles.
pubmed:affiliation
Department of Plant Physiology, University of Lund, P.O. Box 7007, S-220 07 Lund, Sweden.
pubmed:publicationType
Journal Article