Protein profiles of sarcoplasmic reticulum from normal and dystrophic mouse muscle.
Sarcoplasmic reticulum (SR) was isolated from skeletal muscle of dystrophic (C57BL/6J dy2J/dy2J) mice and the protein composition analysed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Densitometric analysis of dystrophic SR preparations indicated a decrease in the Ca2+-ATPase and calsequestrin, and the appearance of a protein with molecular weight 72 000. These differences in the protein profiles between normal and dystrophic SR became more apparent as the disease progressed. The observations are discussed in relation to secondary changes in the dystrophic process such as changes in fibre type and the presence of immature fibres.
D000818:Animals; D002135:Calcium-Binding Proteins / Q000032:analysis; D000252:Calcium-Transporting ATPases / Q000032:analysis; D002155:Calsequestrin / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis; D051379:Mice; D008810:Mice, Inbred C57BL; D008861:Microsomes / Q000032:analysis; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D009136:Muscular Dystrophies / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000032:analysis*
D002135:Calcium-Binding Proteins; D002155:Calsequestrin; D006023:Glycoproteins; D009124:Muscle Proteins; D000252:Calcium-Transporting ATPases