Linked Life Data

823021

Source:http://linkedlifedata.com/resource/pubmed/id/823021

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1976-12-1
pubmed:abstractText
Glycogen synthase a was purified over 500-fold by a procedure which involved solubilisation of the enzyme from a protein-glycogen complex by the action of endogenous phosphorylase and debranching enzyme, followed by DEAE-cellulose chromatography, and either gel filtration on Sepharose 4B or fractionation with polyethylene glycol. 15 mg of protein could be obtained from 1000 g of muscle in five days, corresponding to a yield of 20%. The purity was over 90% as judged by gel electrophoresis and ultracentrifugal analysis. The amino acid composition was determined and the absorption coefficient, A1%280 NM, measured refractiometrically was 13.4. Glycogen synthase a sedimented as two major components, both of which were enzymatically active. The smaller species (13.3 S) comprised 85% and the larger species (19.OS) 15% of the material. The molecular weight of the 13.3-S component was determined to be 377000 by high-speed sedimentation equilibrium centrifugation. The subunit molecular weight measured by gel electrophoresis in the presence of sodium dodecylsulphate was 88 000 indicating that the 13.3-S species is a tetramer. The properties of the enzyme are compared to those obtained by other workers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
68
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-30
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
The purification and properties of rabbit skeletal muscle glycogen synthase.
pubmed:publicationType
Journal Article