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A specific adenosinetriphosphatase of liver mitochondria

A specific adenosinetriphosphatase of liver mitochondria

Journal of Biological Chemistry 200(1): 213-222

The ATPase activity of liver mitochondria was separated from the bulk of the mitochondrial protein and from the adenylate kinase by differential centrifugation of the disintegrated particles. The activity is associated with small particles which are not sedimented in 15 min. at 20,000 X g but are readily sedimented in 30 min. at 110,000 X g. The ATPase in the isolated fraction is specifically activated by Mg and removes only the terminal phosphate of ATP. ADP in concns. comparable to the substrate concn. produces a marked inhibition which was not observed with other phosphate compounds tested. The characteristics of Mg activation and ADP inhibition suggest that a complex of Mg and ATP is the true substrate for the enzyme but that Mg may not be required for combination of enzyme and ATP or ADP.

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Accession: 029793725

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PMID: 13034775

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