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H S PENEFSKY

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PENEFSKY H
Biochem Soc Trans . 1987 Feb; 15(1):97-9. PMID: 2881816
The experiments described in this paper may perhaps point the way towards a reaction mechanism for oxidative phosphorylation. However, we are not yet in a position to write a detailed...
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PENEFSKY H
J Biol Chem . 1985 Nov; 260(25):13735-41. PMID: 2932442
Incubation of [gamma-32P]ATP with a molar excess of the membrane-bound form of mitochondrial ATPase (F1) results in binding of the bulk of the radioactive nucleotide in high affinity catalytic sites...
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PENEFSKY H
J Biol Chem . 1985 Nov; 260(25):13728-34. PMID: 2932441
Submitochondrial particles from beef heart, washed with dilute solutions of KCl so as to activate the latent, membrane-bound ATPase, F1, may be used to study single site catalysis by the...
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PENEFSKY H
Proc Natl Acad Sci U S A . 1985 Mar; 82(6):1589-93. PMID: 2858849
Measurement of the rate of [gamma-32P]ATP binding (k1) and release (k-1) from catalytic sites on submitochondrial particles permitted calculation of the affinity constant in catalytic sites (k1 = K1/k1-1) of...
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PENEFSKY H
Trans N Y Acad Sci . 1983 Jan; 41:139-46. PMID: 6242323
No abstract available.
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Grubmeyer C, CROSS R, PENEFSKY H
J Biol Chem . 1982 Oct; 257(20):12092-100. PMID: 6214557
No abstract available.
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Frangione B, Rosenwasser E, PENEFSKY H, Pullman M
Proc Natl Acad Sci U S A . 1981 Dec; 78(12):7403-7. PMID: 6461003
The complete amino acid sequence of the mitochondrial ATPase inhibitor peptide was determined. The molecule contains 84 residues of which 40 are charged amino acids that occur in clusters along...