Linked Life Data

1829026

Source:http://linkedlifedata.com/resource/pubmed/id/1829026

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-7-26
pubmed:abstractText
Two Ca2(+)-dependent membrane-binding proteins with apparent molecular weights of 70000 (calelectrin70) and 32000 (calelectrin32) were isolated from bovine liver using phenyl-Sepharose affinity chromatography followed by diethylaminoethyl (DEAE)-cellulose and Ultrogel AcA44 chromatographies. Limited proteolysis and immunological analyses indicated that calelectrin32 was not a digested product from calelectrin70. Both calelectrins bound to phosphatidylserine and to calmodulin in a Ca2(+)-dependent manner. Circular dichroism studies showed that the apparent alpha-helical contents of calelectrin70 and calelectrin32 were 25 and 40%, respectively and they underwent Ca2(+)-dependent conformational changes. When the calelectrins were incubated with a brain microtubule preparation, they were phosphorylated by endogenous kinase(s) and phosphorylation occurred on serine residues. Moreover, calelectrin70 showed an inhibitory action on endogenous kinase activity in the presence of Ca2+.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0009-2363
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Structural and functional characterization of calelectrins from bovine liver.
pubmed:affiliation
Faculty of Textile Science and Technology, Shinshu University, Nagano, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't