Erythrocyte spectrin in Duchenne muscular dystrophy.
The primary structure of erythrocyte spectrin bands I and II from controls and patients with Duchenne muscular dystrophy was compared by 2-dimensional peptide mapping. 125I-labelling was done either by the chloramine-T method or using the Bolton and Hunter reagent followed by treatment with trypsin or chymotrypsin, resulting in four different peptide maps from each band of spectrin. Although all the peptide maps of band I were considerably different to those of band II, there were no consistent differences in the maps of bands I and II from controls compared to the corresponding maps from patients with Duchenne muscular dystrophy.
D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000032:analysis*; D006801:Humans; D007202:Indicators and Reagents; D008565:Membrane Proteins / Q000032:analysis*; D009136:Muscular Dystrophies / Q000097:blood*; D010446:Peptide Fragments / Q000032:analysis; D012016:Reference Values; D013049:Spectrin / Q000032:analysis*; D014357:Trypsin
D007202:Indicators and Reagents; D008565:Membrane Proteins; D010446:Peptide Fragments; D013049:Spectrin; D002918:Chymotrypsin; D014357:Trypsin