PMID: 6105877Jul 1, 1980Paper

Highly purified sarcoplasmic reticulum vesicles are devoid of Ca2+-independent ('basal') ATPase activity

Biochimica Et Biophysica Acta
J L FernandezC Hidalgo

Abstract

On solubilization with Triton X-100 of sarcoplasmic reticulum vesicles isolated by differential centrifugation, the Ca2+-ATPase is selectively extracted while approximately half of the initial Mg2+-, or 'basal', ATPase remain in the Triton X-100 insoluble residue. The insoluble fraction, which does not contain the 100 000 dalton polypeptide of the Ca2+-ATPase, contains high levels of cytochrome c oxidase. Furthermore, its Mg2+-ATPase activity is inhibited by specific inhibitors of mitochondrial ATPase, indicating that the 'basal' ATPase separated from the Ca2+-ATPase by detergent extraction originates from mitochondrial contaminants. To minimize mitochondrial contamination, sarcoplasmic reticulum vesicles were fractionated by sedimentation in discontinuous sucrose density gradients into four fractions: heavy, intermediate and light, comprising among them 90-95% of the initial sarcoplasmic reticulum protein, and a very light fraction, which contains high levels of Mg2+-ATPase. Only the heavy, intermediate and light fractions originate from sarcoplasmic reticulum; the very light fraction is of surface membrane origin. Each fraction of sarcoplasmic reticulum origin was incubated with calcium phosphate in the presence of ATP and th...Continue Reading

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