Switch to
Predicate | Object |
---|---|
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-meshheading:8514742-Animals,
pubmed-meshheading:8514742-Cell Membrane,
pubmed-meshheading:8514742-Dystrophin,
pubmed-meshheading:8514742-Electric Organ,
pubmed-meshheading:8514742-Muscle Proteins,
pubmed-meshheading:8514742-Muscles,
pubmed-meshheading:8514742-Nerve Tissue Proteins,
pubmed-meshheading:8514742-Rats,
pubmed-meshheading:8514742-Sarcolemma,
pubmed-meshheading:8514742-Synaptic Membranes,
pubmed-meshheading:8514742-Torpedo
|
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
|