Characterization of the adenosinetriphosphatase and calsequestrin isolated from sarcoplasmic reticulum of normal and dystrophic chickens.
The Ca2+ +Mg2+-dependent adenosinetriphosphatase (EC 3.6.1.3) and calsequestrin have been isolated from the sarcoplasmic reticulum of normal and dystrophic chicken muscle. The adenosinetriphosphatases, isolated from the two lines of chickens were identical in molecular weight, enzyme activity and in Ca2+ +Mg2+-dependence. Calsequestrins isolated from the two lines bound identical amounts of calcium. There were no differences in the Ca2+  transport functions of the sarcoplasmic reticulum membrane, isolated from the two lines of chickens. These results indicate that morphological differences in dystrophic chicken sarcoplasmic reticulum, described by Sabbadini et al (Sabbadini, R., Scales, D. Inesi, G. FEBS Lett. 54, 8 (1975), cannot be ascribed to qualitative differences in the adenosinetriphosphatase or calsequestrin.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology; D002645:Chickens / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism; D009137:Muscular Dystrophy, Animal / Q000378:metabolism*; D010070:Oxalates / Q000494:pharmacology; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*
D009124:Muscle Proteins; D010070:Oxalates; D000251:Adenosine Triphosphatases; D008274:Magnesium; D002118:Calcium