Linked Life Data

6953073

Source:http://linkedlifedata.com/resource/pubmed/id/6953073

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1982-8-7
pubmed:abstractText
An endogenous phosphoryl acceptor has been purified 138-fold from wheat germ extracts. This protein, termed T-substrate, is far more effective than casein or phosvitin as a phosphoryl acceptor for a wheat germ kinase recently purified by our laboratory. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicates that the T-substrate preparation is not homogeneous. The T-substrate, which migrates at a Mr = 48,000, constitutes about 90% of the total protein stain on the gel and is the only protein component which is phosphorylated by the wheat germ kinase. The hydrodynamic properties of the T-substrate have been determined by gel filtration and glycerol density gradient centrifugation. The protein exhibits a Stokes radius of 65.5 A, a sedimentation coefficient of 3.85 S, a frictional ratio of 2.11, and a molecular weight of approximately 104,000. The results suggest that the wheat germ T-substrate is a dimer. The protein exhibits a greater substrate specificity for the wheat germ kinase than for the cyclic AMP-dependent and several independent protein kinases isolated from rabbit skeletal muscle and human erythrocytes. The T-substrate can be maximally phosphorylated by the wheat germ kinase to the extent of about 8 mol of phosphate/48,000 g of protein. Complete dephosphorylation of the phospho-T-substrate occurred upon treatment with phosphatases. The phosphorylated amino acid was identified by high voltage electrophoresis of an acid hydrolysate of 32P-T-substrate. The results indicate that phosphorylation occurs mainly on the seryl residues of T-substrate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7044-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Studies on an endogenous substrate of wheat germ protein kinase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't