Large-scale purification and characterization of the five subunits of F1-ATPase from pig heart mitochondria
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference43 articles.
1. PROTON ATPASES: STRUCTURE AND MECHANISM
2. Structure and function of the ATPase-ATP synthase complex of mitochondria as compared to chloroplasts and bacteria
3. ATP synthesis by oxidative phosphorylation
4. Methods for purification of each subunit of the mitochondrial oligomycin-insensitive adenosine triphosphatase. IV
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1. The nucleotide-independent Fe(III)-binding site is located on β subunit of the mitochondrial F1-ATPase;Biochemical and Biophysical Research Communications;2002-09
2. A Study of the Mitochondrial F1-ATPase Tryptophan Phosphorescence at 273 K;Biochemical and Biophysical Research Communications;1995-02
3. Examination of catalytic activity of the β subunit isolated from chloroplast coupling factor 1;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1994-03
4. Functional nucleotide-binding domain in the F0F1-ATP synthase .alpha. subunit from the yeast Schizosaccharomyces pombe;Biochemistry;1993-10-05
5. Docking the mitochondrial inhibitor protein IF1 to a membrane receptor different from the F1-ATPase beta subunit;European Journal of Biochemistry;1993-07
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