Linked Life Data

3893431

Source:http://linkedlifedata.com/resource/pubmed/id/3893431

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1985-8-9
pubmed:abstractText
Neuraminidase treatment of the purified insulin receptor resulted in an increase in both insulin-binding and kinase activities. Neuraminidase-treated alpha and beta subunits moved further than native subunits on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions. The enhancement of insulin-binding and kinase activities and increased mobility of the subunits on SDS-PAGE were not observed when the receptor was treated with neuraminidase in the presence of neuraminidase inhibitor. These results suggest that terminal sialic acid residues have a significant role in insulin-binding and kinase activities. The involvement of sialic acid residues in the activities of the receptor has not been detected by previous studies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
739-45
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Removal of sialic acids from the purified insulin receptor results in enhanced insulin-binding and kinase activities.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.