Increased phosphorylated components of erythrocyte membrane spectrin band II with reference to Duchenne muscular dystrophy.
Increased erythrocyte band II phosphorylation has been demonstrated in patients with Duchenne muscular dystrophy (DMD). Band II has been purified by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Isoelectric focusing of purified band II from which SDS has been removed reveals heterogeneity. Band II migrates as multiple bands on isoelectric focusing gels and as a single band on SDS-polyacrylamide gels. The increased phosphorylation in DMD does not occur uniformly in all components of band II. Highly phosphorylated components of band II are present in DMD in which only minimal phosphorylation occurs in controls. These results suggest the presence of an abnormal band II substrate in erythrocyte membranes from DMD patients.
D000328:Adult; D001798:Blood Proteins / Q000032:analysis*; D002648:Child; D004910:Erythrocyte Membrane / Q000032:analysis*; D004912:Erythrocytes / Q000032:analysis*; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008297:Male; D009136:Muscular Dystrophies / Q000097:blood*; D013049:Spectrin / Q000032:analysis*
D001798:Blood Proteins; D013049:Spectrin