Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma
作者： K Ohlendieck , J M Ervasti , J B Snook , K P Campbell
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摘要: mAbs specific for protein components of the surface membrane rabbit skeletal muscle have been used as markers in isolation and characterization sarcolemma membranes. Highly purified membranes from were isolated a crude preparation by wheat germ agglutination. Immunoblot analysis subcellular fractions revealed that dystrophin its associated glycoproteins 156 50 kD are greatly enriched vesicles. The was also novel (SL45, SL/TS230) Na+/K(+)-ATPase, whereas t-tubule (alpha 1 alpha 2 subunits dihydropyridine receptor, TS28) sarcoplasmic reticulum (Ca2(+)-ATPase, ryanodine receptor) diminished this preparation. Analysis SDS-PAGE densitometric scanning demonstrated made up 2% total Therefore, our results demonstrate although is minor it major constituent muscle. Thus absence Duchenne muscular dystrophy may result disruption cytoskeletal network underlying dystrophic
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