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Identification of abnormally [³²P]-phosphorylated cyanogen bromide cleavage product of erythrocyte membrane spectrin in Duchenne muscular dystrophy

Howard Hughes Medical Institute (Dr. Roses and Mr. Herbstreith), Departments of Medicine (Neurology) (Dr. Roses, Mr. Shile, Mr. Herbstreith, and Dr. Balakrishnan), and Biochemistry (Dr. Roses), Duke University Medical Center, Durham, NC.

Address correspondence and reprint requests to Dr. Roses, Box 2900, Duke University Medical Center, Durham, NC 27710.

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.