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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1995-4-13
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Cobalt,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Ethers, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
208
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
274-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7887940-Amino Acid Sequence,
pubmed-meshheading:7887940-Animals,
pubmed-meshheading:7887940-Antibodies,
pubmed-meshheading:7887940-Cations, Divalent,
pubmed-meshheading:7887940-Cattle,
pubmed-meshheading:7887940-Cobalt,
pubmed-meshheading:7887940-Edetic Acid,
pubmed-meshheading:7887940-Egtazic Acid,
pubmed-meshheading:7887940-Enzyme Activation,
pubmed-meshheading:7887940-Enzyme Stability,
pubmed-meshheading:7887940-Ethers, Cyclic,
pubmed-meshheading:7887940-Freezing,
pubmed-meshheading:7887940-Isoenzymes,
pubmed-meshheading:7887940-Kinetics,
pubmed-meshheading:7887940-Manganese,
pubmed-meshheading:7887940-Molecular Sequence Data,
pubmed-meshheading:7887940-Myocardium,
pubmed-meshheading:7887940-Okadaic Acid,
pubmed-meshheading:7887940-Oligopeptides,
pubmed-meshheading:7887940-Phosphoprotein Phosphatases,
pubmed-meshheading:7887940-Protein Phosphatase 1,
pubmed-meshheading:7887940-Protein Phosphatase 2
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pubmed:year |
1995
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pubmed:articleTitle |
A metal-dependent form of protein phosphatase 2A.
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pubmed:affiliation |
Department of Pharmacology Medical College of Ohio, Toledo 43699.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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