Linked Life Data

9016848

Source:http://linkedlifedata.com/resource/pubmed/id/9016848

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-5-29
pubmed:abstractText
We have already described the separation of two brain soluble fractions by Sephadex G-50, one of which stimulates (peak I) and the other inhibits (peak II) Na+, K(+)-ATPase and K(+)-p-nitrophenylphosphatase (K(+)-p-NPPase) activities. Here we examine the features of synaptosomal membrane p-NPPase activity in the presence and absence of brain peak I. It was observed that stimulation of Mg2+, K(+)-p-NPPase activity by peak I was concentration dependent. The ability of peak I to stimulate p-NPPase activity was lost by heat treatment followed by brief centrifugation. Pure serum albumin also stimulated enzyme activity. K(+)-p-NPPase stimulation by peak I proved dependent on K+ concentration but independent of Mg2+ and substrate p-nitrophenylphosphate concentrations. Since our determinations were performed in a non-phosphorylating condition reflecting the Na+, K(+)-ATPase Na+ site, it is suggested that peak I may stimulate the Na+-dependent enzyme phosphorylation known to take place from the internal cytoplasmic side.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0364-3190
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Kinetics of K(+)-p-nitrophenyl phosphatase stimulation by a brain soluble fraction.
pubmed:affiliation
Instituto de Biologia Cellular y Neurociencias Prof. Eduardo De Robertis, Facultad de Medicina, Universidad de Buenos Aires, Paraguay, Argentina.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't