Linked Life Data

3008662

Source:http://linkedlifedata.com/resource/pubmed/id/3008662

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-5-12
pubmed:abstractText
The calmodulin- and cAMP-dependent protein kinase-mediated phosphorylations of isolated sarcolemma and sarcoplasmic reticulum vesicles have been compared. Similarities in the calmodulin-mediated phosphorylation of the sarcolemma and sarcoplasmic reticulum 23,000-Da phosphoproteins included their Mg2+, Na+, Ca2+, and calmodulin sensitivities, as well as the size of their dissociated subunits. In contrast, a number of differences between these phosphoproteins were indicated in their sensitivity to detergents (Triton X-100 and sodium dodecyl sulfate) and calmodulin antagonists (R24571 and trifluoperazine). Furthermore, in contrast to the sarcoplasmic reticulum phosphoprotein, the sarcolemma phosphoprotein could not be affinity labeled with 125I-calmodulin. While these results indicate the probable chemical similarity of the sarcolemma and sarcoplasmic reticulum 23,000-Da phosphoproteins, they also indicate there are differences in the lipid/phosphoprotein interactions in these two membranes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
246
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
98-107
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Properties of the 23,000-Da phosphoproteins in cardiac sarcolemma and sarcoplasmic reticulum.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't