| pubmed-article:9016848 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9016848 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:9016848 | lifeskim:mentions | umls-concept:C1166626 | lld:lifeskim |
| pubmed-article:9016848 | lifeskim:mentions | umls-concept:C0031678 | lld:lifeskim |
| pubmed-article:9016848 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:9016848 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:9016848 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9016848 | pubmed:dateCreated | 1997-5-29 | lld:pubmed |
| pubmed-article:9016848 | 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. | lld:pubmed |
| pubmed-article:9016848 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9016848 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9016848 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9016848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9016848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9016848 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9016848 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9016848 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9016848 | pubmed:issn | 0364-3190 | lld:pubmed |
| pubmed-article:9016848 | pubmed:author | pubmed-author:Rodríguez... | lld:pubmed |
| pubmed-article:9016848 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9016848 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:9016848 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9016848 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9016848 | pubmed:pagination | 215-9 | lld:pubmed |
| pubmed-article:9016848 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:meshHeading | pubmed-meshheading:9016848-... | lld:pubmed |
| pubmed-article:9016848 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9016848 | pubmed:articleTitle | Kinetics of K(+)-p-nitrophenyl phosphatase stimulation by a brain soluble fraction. | lld:pubmed |
| pubmed-article:9016848 | pubmed:affiliation | Instituto de Biologia Cellular y Neurociencias Prof. Eduardo De Robertis, Facultad de Medicina, Universidad de Buenos Aires, Paraguay, Argentina. | lld:pubmed |
| pubmed-article:9016848 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9016848 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
