Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1993-7-22
pubmed:abstractText
Using solubilized dystrophin isolated from torpedo electric tissue and in vitro blot overlay assay, we have identified dystrophin-binding proteins in membranes from Torpedo electrocyte and rat muscle. In acetylcholine receptor-rich membranes from Torpedo marmorata electric tissue, an extrinsic protein of M(r) 52,000, known as the 58-kDa protein (Froehner, S.C. (1984) J. Cell Biol. 99, 88-96), represents the major binding site for dystrophin. When membranes were solubilized by non-ionic detergents, the 52-kDa protein as well as a few proteins of M(r) 200,000, 87,000, and 45,000 co-extract and copurify with dystrophin. In rat sarcolemma, a protein doublet of approximately 58-60 kDa also binds dystrophin in vitro, this protein likely being the DAP 59 characterized by Ervasti and Campbell (Ervasti, J. M., and Campbell, K. P. (1991) Cell 66, 1121-1131). We postulate that the 52- and 59-kDa proteins are functional homologs that play the role of "receptors" for dystrophin in various specialized membrane domains.
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
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13019-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Identification of dystrophin-binding protein(s) in membranes from Torpedo electrocyte and rat muscle.
pubmed:affiliation
Département de Biologie Supramoléculaire et Cellulaire, Institut Jacques Monod, Centre National de la Recherche Scientifique, Université Paris VII, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't