The stoichiometry of the iron-sulphur clusters 1a, 1b and 2 of NADH:Q oxidoreductase as present in beef-heart submitochondrial particles.
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Animals↗
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Ca2+-regulated release of an ATPase inhibitor protein from submitochondrial particles derived from skeletal muscles of the rat.
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Adenosine Triphosphatases↗
THE SUCCINATE-LINKED NICOTINAMIDE-ADENINE DINUCLEOTIDE REDUCTION IN SUBMITOCHONDRIAL PARTICLES. I. KINETIC STUDIES OF THE REACTION.
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Adenine Nucleotides↗
RESTORATION OF OXIDATIVE PHOSPHORYLATION IN NON-PHOSPHORYLATING SUBMITOCHONDRIAL PARTICLES BY OLIGOMYCIN.
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Adenosine Triphosphatases↗
The recognition of two specific binding sites of the adenine nucleotide translocase by palmitoyl CoA in bovine heart mitochondria and submitochondrial particles.
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Acyl Coenzyme A↗
Inhibition of beta-hydroxybutyrate oxidation in rat liver mitochondria or submitochondrial particles by monocarboxylates transport inhibitors.
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Animals↗
A Ca2+-binding lipoprotein from submitochondrial particles of rat skeletal muscle or bovine heart.
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Adenosine Triphosphatases↗
The membrane in submitochondrial particles protects F1-ATPase from trinitrobenzolsulphonate and dinitrofluorobenzole.
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Animals↗
THE SUCCINATE-LINKED NICOTINAMIDE-ADENINE DINUCLEOTIDE REDUCTION IN SUBMITOCHONDRIAL PARTICLES. II. STUDIES WITH INHIBITORS.
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Adenosine Triphosphate↗
ON THE MECHANISM OF OXIDATIVE PHOSPHORYLATION. 8. FURTHER EVIDENCE FOR DISTINCT TRANSHYDROGENASE REACTIONS IN SUBMITOCHONDRIAL PARTICLES.
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Adenosine Triphosphate↗
The Maxwell demon in biological systems. Use of glucose 6-phosphate and hexokinase as an ATP regenerating system by the Ca(2+)-ATPase of sarcoplasmic reticulum and submitochondrial particles.
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Adenosine Diphosphate↗
Preparation and characterization of mitochondria and submitochondrial particles of rat liver and liver-derived tissues.
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Adenosine Triphosphatases↗
The electrogenic nature of ADP/ATP transport in inside-out submitochondrial particles.
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Adenosine Diphosphate↗
SUCCINATE-LINKED NICOTINAMIDE-ADENINE DINUCLEOTIDE REDUCTION COUPLED WITH THE AEROBIC OXIDATION OF REDUCED TETRAMETHYL-P-PHENYLENEDIAMINE IN SUBMITOCHONDRIAL PARTICLES.
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Adenosine Triphosphate↗
Generation of high delta psi in respiring submitochondrial particles by steady-state accumulation of oxidized N,N,N',N'-tetramethyl-p-phenylenediamine.
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Animals↗
Hormones and liver mitochondria: effects of growth hormone and thyroxine on respiration, fluorescence of 1-anilino-8-naphthalene sulfonate and enzyme activities of complex I and II of submitochondrial particles.
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Anilino Naphthalenesulfonates↗
Titration of the binding sites for the oligomycin-sensitivity conferring protein in beef heart submitochondrial particles.
The binding parameters of the oligomycin-sensitivity conferring protein (OSCP) in inside-out particles from beef heart mitochondria have been tested by means of two assays, the oligomycin-sensitive ATP-Pi exchange, and the oligomycin-sensitive ATP hydrolysis. The total number of OSCP binding sites in A particles was equal to 220 pmol/mg particle protein. Each mole of ATPase active site was able to bind 1.1 +/- 0.5 mol OSCP with Kd 1.7 nM.
Adenosine Triphosphatases↗
Initiation of lipid peroxidation in submitochondrial particles: effect of respiratory inhibitors.
Initiation of lipid peroxidation in the inner mitochondrial membrane was investigated using respiratory substrates and inhibitors and various iron chelates. An iron chelate was required for initiation of lipid peroxidation in the presence of either NADH or NADPH. The two nicotinamide nucleotides exhibited different activities in initiating lipid peroxidation with regard to concentration and to the effects of rotenone and rhein. Succinate and both nicotinamide nucleotides supported lipid peroxidation in the presence of thenoyl trifluoroacetone (TTFA), without a requirement for exogenously added iron. ADP stimulated lipid peroxidation in the case of NAD(P)H and TTFA, but inhibited it in the case of succinate and TTFA. Lipid peroxidation is thought to be enzymatically induced in both the NADH and the succinate dehydrogenase regions of the respiratory chain, and evidence is presented for a novel pathway of NADPH oxidation that may also be involved. Possible initiation mechanisms are discussed.
Adenosine Diphosphate↗