| Literature DB >> 2556382 |
H W Chang1, E Bock, E Bonilla.
Abstract
We have found that dystrophin is highly concentrated at neuromuscular junctions and innervated membranes of the electric organ of Torpedo californica. In acetylcholine receptor-rich Torpedo membrane preparations dystrophin represents approximately 0.4% of total protein and can be extracted from these membranes by alkaline treatment in the absence of detergent, indicating that it is a peripheral membrane protein. Polyclonal antibodies raised against electrophoretically isolated Torpedo dystrophin cross-react with dystrophin in human muscle and unequivocally discriminate between normal and Duchenne muscular dystrophy patient's muscle. These results indicate that dystrophin is phylogenetically a highly conserved protein and that the relatively abundant dystrophin in electric organ would facilitate further investigations of its structure and function.Entities:
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Year: 1989 PMID: 2556382
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157