Identification of dystrophin in cardiac sarcolemmal vesicles.
We have identified dystrophin in highly purified sarcolemmal vesicles isolated from canine and bovine hearts using specific antibodies against the COOH-terminal region of the protein. Bovine cardiac sarcolemma contained a single immunoreactive protein band (Mr. approximately 400,000) whereas the canine cardiac membrane contained a doublet (Mr. approximately 420,000 and approximately 380,000). The higher molecular weight form of canine cardiac dystrophin was more abundant than the lower molecular weight form. These highly purified preparations of the sarcolemmal vesicles should provide a useful tool for structural and functional analysis of the interaction of dystrophin with the plasma membrane.
Michalak
M
M
Department of Pediatrics, University of Alberta, Edmonton, Canada.
Zubrzycka-Gaarn
E
E
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D015415:Biomarkers / Q000032:analysis*; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002458:Cell Fractionation; D004285:Dogs; D016189:Dystrophin; D008024:Ligands; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D009206:Myocardium / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D012508:Sarcolemma / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D012964:Sodium / Q000378:metabolism
D000906:Antibodies; D000936:Antigen-Antibody Complex; D015415:Biomarkers; D016189:Dystrophin; D008024:Ligands; D009124:Muscle Proteins; D012964:Sodium; D000251:Adenosine Triphosphatases; D002118:Calcium