Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1982-12-2
pubmed:abstractText
Separation 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.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
950-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
[Characterization of endogenous phosphorylation substrates of sarcoplasmic reticulum fragments from fast skeletal muscles of the rabbit].
pubmed:publicationType
Journal Article, English Abstract