Linked Life Data

2373153

Source:http://linkedlifedata.com/resource/pubmed/id/2373153

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-8-28
pubmed:abstractText
Two bovine lens plasma membrane proteins have been identified that bind calmodulin in a Ca2(+)-dependent fashion. Electrophoretic analysis of lens membrane proteins photoaffinity-labeled with benzophenone[125I]calmodulin confirmed our previous observation [Louis, Johnson and Turnquist (1985) Eur. J. Biochem. 150, 271-8] that two major products are formed with Mr = 46 kDa and 36 kDa. Limited proteolysis of lens membrane proteins with chymotrypsin resulted in the formation of a 21-kDa-fragment that was derived from the hydrolysis of the major lens membrane protein MP26; this correlated with the loss of the 46-kDa complex, and the formation of a 41-kDa photoaffinity-labeled complex. Use of the [125I]calmodulin gel overlay procedure confirmed that the 46-kDa and 41-kDa photoaffinity-labeled complexes reflect the interaction of calmodulin with both MP26 and its 21-kDa chymotryptic fragment, respectively. Proteolysis of lens membranes with higher concentrations of chymotrypsin resulted in the hydrolysis of the 18-kDa protein which correlated with the generation of a 12-kDa fragment; this paralleled the loss of the 36-kDa photoaffinity labeled complex and the formation of a 28-kDa-complex. The [125I]calmodulin gel overlay procedure demonstrated that the 36-kDa and 28-kDa photoaffinity-labeled complexes reflect the interaction of calmodulin with the 18-kDa lens membrane protein and its likely 12-kDa chymotryptic fragment, respectively. Identification of these calmodulin-binding proteins suggests that MP26 and the 18-kDa membrane protein are likely candidates for the proposed calcium sensitive, calmodulin-dependent gating of lens fiber cell junctions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-4835
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
495-503
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Identity of the calmodulin-binding proteins in bovine lens plasma membranes.
pubmed:affiliation
Department of Veterinary Biology, University of Minnesota, St Paul 55108.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.