| pubmed-article:7887940 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7887940 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:7887940 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:7887940 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7887940 | pubmed:dateCreated | 1995-4-13 | lld:pubmed |
| pubmed-article:7887940 | pubmed:abstractText | Highly purified bovine heart protein phosphatase 2A catalytic subunit lost virtually all of its activity during storage at -70 degrees. When the enzyme was preincubated with Co2+, over 35% of the original activity was restored. Freshly prepared protein phosphatase 2A purified from bovine heart was stimulated at least 3 to 4-fold by pretreatment with Co2+ or Mn2+. Activation by Co2+ appeared to be irreversible whereas activation by Mn2+ was partially reversed after the cation was chelated with excess EDTA/EGTA. The sensitivity of Co2(+)-stimulated protein phosphatase 2A to okadaic acid or inhibitor-2 was similar to that of spontaneously active protein phosphatase 2A. The enzyme was converted to a latent form by treatment with phosphate or pyrophosphate. The latent form was completely reactivated by preincubation with Co2+. These results demonstrate that protein phosphatase 2A, like phosphatase 1, can exist in a metal ion-dependent form and may represent a new mechanism for the regulation of protein phosphatase 2A activity. | lld:pubmed |
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| pubmed-article:7887940 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7887940 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7887940 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7887940 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7887940 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:7887940 | pubmed:author | pubmed-author:WilsonS ESE | lld:pubmed |
| pubmed-article:7887940 | pubmed:author | pubmed-author:ChoCC | lld:pubmed |
| pubmed-article:7887940 | pubmed:author | pubmed-author:SchlenderK... | lld:pubmed |
| pubmed-article:7887940 | pubmed:author | pubmed-author:CauPP | lld:pubmed |
| pubmed-article:7887940 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7887940 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:7887940 | pubmed:volume | 208 | lld:pubmed |
| pubmed-article:7887940 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7887940 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7887940 | pubmed:pagination | 274-9 | lld:pubmed |
| pubmed-article:7887940 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:7887940 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7887940 | pubmed:articleTitle | A metal-dependent form of protein phosphatase 2A. | lld:pubmed |
| pubmed-article:7887940 | pubmed:affiliation | Department of Pharmacology Medical College of Ohio, Toledo 43699. | lld:pubmed |
| pubmed-article:7887940 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7887940 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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