pubmed-article:8910475 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8910475 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:8910475 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8910475 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
pubmed-article:8910475 | pubmed:issue | 45 | lld:pubmed |
pubmed-article:8910475 | pubmed:dateCreated | 1996-12-30 | lld:pubmed |
pubmed-article:8910475 | pubmed:abstractText | Biotinylated microcystin was used to affinity purify over avidin-Sepharose the entire cellular content of active forms of protein phosphatase (PP) 1 and 2A holoenzymes present in three subcellular fractions of skeletal muscle. Biotinylated microcystin displayed IC50 values in the nM range against PP-1C (1.58 +/- 0.6 nM S.E., n = 3), PP-2AC (0.63 +/- 0.2 nM S.E., n = 3) and SMPP-1M (5.9 +/- 1.3 S.E., n = 3). Subsequent anion-exchange chromatography and SDS-polyacrylamide gel electrophoresis of the microcystin-biotin eluates of the three fractions revealed a complex pattern of proteins associated with PP-1C and PP-2AC. Far Western analysis and the rebinding interaction with recombinant PP-1C distinguished proteins in the eluates that bound PP-1C from those that bound PP-2AC. In Far Western analysis, 29 distinct proteins were identified to bind PP-1C. Significantly, these same proteins, plus seven others, were also recovered from the isothiocyanate eluates from microcystin-Sepharose by a rebinding interaction with PP-1C-microcystin-biotin. The number of proteins and range of novel molecular masses (18-125 kDa) identified to interact with PP-1C by these two techniques cannot be accounted for by the previously characterized subunits of PP-1. Our findings further support the concept that PP-1C is regulated in vivo by multiple and distinct substrate-targeting subunits. | lld:pubmed |
pubmed-article:8910475 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:language | eng | lld:pubmed |
pubmed-article:8910475 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8910475 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8910475 | pubmed:month | Nov | lld:pubmed |
pubmed-article:8910475 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:8910475 | pubmed:author | pubmed-author:CamposMM | lld:pubmed |
pubmed-article:8910475 | pubmed:author | pubmed-author:QianZZ | lld:pubmed |
pubmed-article:8910475 | pubmed:author | pubmed-author:HaysteadT ATA | lld:pubmed |
pubmed-article:8910475 | pubmed:author | pubmed-author:FaddenPP | lld:pubmed |
pubmed-article:8910475 | pubmed:author | pubmed-author:AlmsGG | lld:pubmed |
pubmed-article:8910475 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8910475 | pubmed:day | 8 | lld:pubmed |
pubmed-article:8910475 | pubmed:volume | 271 | lld:pubmed |
pubmed-article:8910475 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8910475 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8910475 | pubmed:pagination | 28478-84 | lld:pubmed |
pubmed-article:8910475 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:8910475 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8910475 | pubmed:articleTitle | Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography. | lld:pubmed |
pubmed-article:8910475 | pubmed:affiliation | Department of Pharmacology, and Markey Center for Cell Signaling, University of Virginia, Charlottesville, Virginia 22908, USA. | lld:pubmed |
pubmed-article:8910475 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8910475 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8910475 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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