Analysis of rabbit skeletal-muscle microsomal proteins [proceedings].
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Biomedical subjects
Publications and source records attributed to D R Headon.
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The composition of skeletal muscle microsomes is reviewed. Evidence for the involvement of cholesterol in the transport of calcium by vesicles derived from the sarcoplasmic reticulum is considered. Results obtained by non aqueous extractions of skeletal muscle microsomes, and by use of the cholesterol analogue 20, 25 diazacholesterol indicate that cholesterol is not involved in calcium transport by vesicles of sarcoplasmic reticulum origin. Use of density perturbation procedures indicating that cholesterol is present in muscle membranes other than those of the sarcoplasmic reticulum involved in calcium transport is discussed. The distribution of membranal cholesterol in muscle is compared to that in other tissues.
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Basal ATPase is readily separated from the Ca2+-ATPase of the sarcoplasmic reticulum. The median density distributions of cholesterol and basal ATPase activities are almost identical. Digitonin has been successfully employed in determining the association of cholesterol with specific vesicles in rat liver microsomal preparations. Treatment of rabbit skeletal muscle microsomal preparations with digitonin alters the density distribution patterns of basal ATPase activity and cholesterol in an identical fashion. Protein distribution displays a less marked change in median density. Enzymic activity associated with calcium transport, measured under differing conditions, is largely unaffected. It is concluded that cholesterol and basal ATPase activity are associated with a distinct group of rabbit skeletal muscle microsomal particles.
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