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Increased (/sup 32/P)-phosphorylation of tryptic peptides of erythrocyte spectrin in Duchenne muscular dystrophy

Journal Article · · Muscle Nerve; (United States)
OSTI ID:5245930
Increased (32P)-incorporation in tryptic peptides of the erythrocyte membrane protein spectrin Band 2 in Duchenne muscular dystrophy (DMD) was studied in a consecutive series of 10 matched DMD/control pairs. Spectrin was (32P)-phosphorylated by cyclic AMP-independent endogenous membrane protein kinase in the presence of (gamma-32P)ATP. (32P)-labeled spectrin was isolated, purified, and subjected to tryptic cleavage with excess trypsin. The resulting peptides were separated on a high-resolution 5%/15% stacking SDS--polyacrylamide gel electrophoresis system. Liquid scintillation counting was performed on sequential slices of unstained gels. A broad (32P)-labeled band containing a number of (32P)-polypeptides was found to be more highly (32P)-phosphorylated in DMD patients than in their matched controls. This band migrated with an apparent molecular mass of 4.8-5.2 kilodaltons and contained approximately 55% of total (32P) radioactivity covalently bound to spectrin peptides. These data demonstrated an increased (32P)-phosphorylation of an identifiable tryptic peptide fraction in DMD that is consistent with previous reports of increased spectrin Band 2 (32P)-phosphorylation in DMD.
Research Organization:
Department of Medicine, Duke University Medical Center, Howard Hughes Medical Institute, Durham, NC
OSTI ID:
5245930
Journal Information:
Muscle Nerve; (United States), Journal Name: Muscle Nerve; (United States) Vol. 4:6; ISSN MUNED
Country of Publication:
United States
Language:
English