Interaction between bleomycin and glutathione in cancer-bearing animals.
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Biomedical subjects
Publications and source records attributed to T Kaneda.
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An acetate-requiring leaky mutant was induced from Bacillus subtilis 168, and activities of its three alpha-keto acid dehydrogenases were compared with the respectives activities of the parent strain. Both pyruvate and alpha-ketoisovalerate dehydrogenase activities in the mutant were consideralby lower, being only 10-17% of those of the parent, but alpha-ketoglutarate dehydrogenase activity was unchanged. These dehydrogenases are complexed composed of three enzymes: a carboxylase, a lipoic reductase-transacylase, and a dihydrolipoyl dehydrogenase. The carboxylase activity of the affected complexes was no different. Total dihydrolipoyl dehydrogenase activity was only one-third. Thus dihydrolipoyl dehydrogenase is the defective enzyme in the two dehydrogenase complexes; the activity remaining in the mutant is accounted for by the activity of the intact alpha-ketoglutarate dehydrogenase.
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