A chromatographic and electrophoretic study of sarcoplasm from adult- and foetal-rabbit muscles

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Abstract
Rabbit skeletal muscle has been fractionated by chromatography on di-ethylaminoethylcellulose at pH 7.6 and 9.3. On starch-gel electro -ohoresis of adult-rabbit skeletal muscle at least 15 migrating bands have been recognized and some of them identified with known proteins. The more positively charged protein components which are readily eluted from diethylaminoethylcellulose are relatively much decreased in sarcoplasm isolated from foetal-rabbit skeletal muscle and from adult heart muscle compared with the amounts present in the corresponding fraction from adult skeletal muscle. The level of aldolase activity in foetal-skeletal muscle sarcoplasm is comparable with that in adult-heart-muscle sarcoplasm but much lower than that found in adult-rabbit skeletal muscle sarcoplasm.