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Oxidation of NADPH by submitochondrial particles from beef heart in complete absence of transhydrogenase activity from NADPH to NAD

The Journal of Biological Chemistry

Dec 25, 1975

L Djavadi-Ohaniance, H Hatefi

PMID: 395

Abstract

Treatment of submitochondrial particles (ETP) with trypsin at 0 degrees destroyed NADPH leads to NAD (or 3-acetylpyridine adenine dinucleotide, AcPyAD) transhydrogenase activity. NADH oxidase activity was unaffected; NADPH oxidase and NADH leads to AcPyAD transhydrogenase activities wer...read more

Mentioned in this Paper

Dysplastic Nevus
Metabolic Inhibition
Iron-Sulfur Proteins
Ligands
Complex (molecular entity)
Binding Protein
Mitochondria, Heart
Mitochondria, Muscle
Anions
Myocardium
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Oxidation of NADPH by submitochondrial particles from beef heart in complete absence of transhydrogenase activity from NADPH to NAD

The Journal of Biological Chemistry

Dec 25, 1975

L Djavadi-Ohaniance, H Hatefi

PMID: 395

DOI:

Abstract

Treatment of submitochondrial particles (ETP) with trypsin at 0 degrees destroyed NADPH leads to NAD (or 3-acetylpyridine adenine dinucleotide, AcPyAD) transhydrogenase activity. NADH oxidase activity was unaffected; NADPH oxidase and NADH leads to AcPyAD transhydrogenase activities wer...read more

Mentioned in this Paper

Dysplastic Nevus
Metabolic Inhibition
Iron-Sulfur Proteins
Ligands
Complex (molecular entity)
Binding Protein
Mitochondria, Heart
Mitochondria, Muscle
Anions
Myocardium

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