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The Subunit Structure of Beef Heart Mitochondrial Adenosine Triphosphatase

PHYSICAL AND CHEMICAL PROPERTIES OF ISOLATED SUBUNITS

From the ¹ From the Department of Biochemistry, The Public Health Research Institute of The City of New York, Inc., New York, New York 10016

The isolated subunits of beef heart mitochondrial ATPase were characterized with regard to physical and chemical properties. Three subunits, molecular weight 54,000, 50,000, and 33,000, respectively, constituted 93% of the protein of the oligomer. The remainder of the molecule consisted of two subunits of molecular weight 17,300 and 5,700. The latter peptide (Subunit 5) was identified by physical criteria with the ATPase inhibitor of Pullman and Monroy (Pullman, M. E., and Monroy, G. (1963) J. Biol. Chem. 238, 3762–3769). Subunit 5 was a basic protein (pI = 10.4) which was removed from the ATPase in the form of a mixture of monomer (5,700) and dimer (11,350). Conversion of the dimer to the monomer was dependent on the presence of agents capable of reducing disulfide bonds.

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