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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1990-10-9
|
| pubmed:abstractText |
The preparation of the purified Ca2+, Mg2(+)-ATPase has been isolated from triton X-100 solubilizate of plasma membranes of the pig myometrium using the method of affinity chromatography on calmodulin-Sepharose 4B. The specific activity of the enzyme shows its 52-fold purification. The enzymic preparation practically has no Mg2(+)-ATPase activity. By the data of DS-Na-electrophoresis in PAAG the Ca2+, Mg2+ ATPase preparation consists of two polypeptides with Mm 130 and 205 kDa. Autoradiography shows their Ca2(+)-dependent phosphorylation. The purified enzyme is highly sensitive to the inhibitory effect of orthovanadate.
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0201-8470
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
62
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
60-5
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:2144381-Animals,
pubmed-meshheading:2144381-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:2144381-Calcium-Transporting ATPases,
pubmed-meshheading:2144381-Cell Membrane,
pubmed-meshheading:2144381-Chromatography, Affinity,
pubmed-meshheading:2144381-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2144381-Female,
pubmed-meshheading:2144381-Myometrium,
pubmed-meshheading:2144381-Solubility,
pubmed-meshheading:2144381-Swine
|
| pubmed:articleTitle |
[Isolation and purification of Ca2+,Mg2+-ATPase from plasma membranes of the myometrium].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|