Identification of abnormally [32P]-phosphorylated cyanogen bromide cleavage product of erythrocyte membrane spectrin in Duchenne muscular dystrophy.
We measured [32P]-phosphorylation of erythrocyte membrane spectrin band 2 peptides from patients with Duchenne muscular dystrophy. Erythrocyte ghosts were prepared and subjected to [32P]-phosphorylation by endogenous protein kinase incubations. Purified spectrin was then cleaved by cyanogen bromide, and the resulting peptides were analyzed by electrophoresis on 5%/15% SDS polyacrylamide stacking slab and tube gel systems. More than 50% of the incorporated [32P] was associated with a single band, CN-A, with an apparent molecular weight of 23 kilodaltons. The Coomassie blue-stained peptides were identical in patients and controls. Band CN-A represented approximately 2% of the total peptide protein but was more [32P]-phosphorylated in patients than in controls.
D001345:Autoradiography; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D009136:Muscular Dystrophies / Q000097:blood*; D010766:Phosphorylation; D013049:Spectrin / Q000032:analysis*
D008565:Membrane Proteins; D013049:Spectrin; D003488:Cyanogen Bromide