Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:7115808rdf:typepubmed:Citationlld:pubmed
pubmed-article:7115808lifeskim:mentionsumls-concept:C0034493lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C0242692lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C0036226lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C0031715lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C0486805lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C1710236lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C0456962lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C1880022lld:lifeskim
pubmed-article:7115808lifeskim:mentionsumls-concept:C0205227lld:lifeskim
pubmed-article:7115808pubmed:issue6lld:pubmed
pubmed-article:7115808pubmed:dateCreated1982-12-2lld:pubmed
pubmed-article:7115808pubmed:abstractTextSeparation of phosphorylated sarcoplasmic reticulum (SR) fragments by polyacrylamide gel disc electrophoresis in the presence of Na-DS revealed that the radioactivity is distributed in protein zones with molecular weights of 95,000 and 6000-8000. The phosphorylation of the protein with m. w. of 95,000 is Ca2+-dependent. The tryptic hydrolysis of the phosphorylated SR fragments from fast skeletal muscles results in a loss of radioactivity by 60-70%; phospholipase C from Clostridium welchii reduces the labelled phosphate content by 40-50%. The cAMP-dependent protein kinase inhibitor decreases the phosphorylation of both substrates. The substrate of phosphorylation with m. w. of 6000-8000 is not stained with Amidoschwartz 10B or Coumassie brilliant blue. Extraction by an acidified chlorophorm--methanol mixture results in a proteolipid with specific radioactivity exceeding that of the original preparation of phosphorylated SR membranes 3-4-fold. Thin-layer chromatography on Silufol plates and Silicagel KSK showed that the proteolipid is not chromatographically homogeneous after 2-fold precipitation by diethyl ether and is localized in a band with Rf varying from 0.6 to 0.8. The fluorescence spectrum of the proteolipid in a chlorophorm--methanol--HCl solution is represented by an assymmetrical structure-free band with a maximum at 350 nm. A possible role of phosphorylase b and proteolipid in manifestation of the functional activity of the SR fragments is discussed.lld:pubmed
pubmed-article:7115808pubmed:languageruslld:pubmed
pubmed-article:7115808pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7115808pubmed:citationSubsetIMlld:pubmed
pubmed-article:7115808pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7115808pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7115808pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7115808pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7115808pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7115808pubmed:statusMEDLINElld:pubmed
pubmed-article:7115808pubmed:monthJunlld:pubmed
pubmed-article:7115808pubmed:issn0320-9725lld:pubmed
pubmed-article:7115808pubmed:authorpubmed-author:Kurski?M DMDlld:pubmed
pubmed-article:7115808pubmed:authorpubmed-author:KondratiukT...lld:pubmed
pubmed-article:7115808pubmed:authorpubmed-author:LitvinenkoE...lld:pubmed
pubmed-article:7115808pubmed:authorpubmed-author:FedorovA NANlld:pubmed
pubmed-article:7115808pubmed:authorpubmed-author:MeshkovaL ILIlld:pubmed
pubmed-article:7115808pubmed:authorpubmed-author:OsipenkoA AAAlld:pubmed
pubmed-article:7115808pubmed:issnTypePrintlld:pubmed
pubmed-article:7115808pubmed:volume47lld:pubmed
pubmed-article:7115808pubmed:ownerNLMlld:pubmed
pubmed-article:7115808pubmed:authorsCompleteYlld:pubmed
pubmed-article:7115808pubmed:pagination950-6lld:pubmed
pubmed-article:7115808pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:meshHeadingpubmed-meshheading:7115808-...lld:pubmed
pubmed-article:7115808pubmed:year1982lld:pubmed
pubmed-article:7115808pubmed:articleTitle[Characterization of endogenous phosphorylation substrates of sarcoplasmic reticulum fragments from fast skeletal muscles of the rabbit].lld:pubmed
pubmed-article:7115808pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7115808pubmed:publicationTypeEnglish Abstractlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7115808lld:pubmed