JBC Avanti Polar Lipids

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Mammalian agr-Keto Acid Dehydrogenase Complexes

I. ISOLATION, PURIFICATION, AND PROPERTIES OF PYRUVATE DEHYDROGENASE COMPLEX OF PIG HEART MUSCLE

Taro Hayakawa 1, Masahiro Hirashima 1, Satoshi Ide 1, Minoru Hamada 1, Keiichiro Okabe 1, and Masahiko Koike 1

From the 1 From the Department of Pathological Biochemistry, Atomic Disease Institute, Nagasaki University School of Medicine, Sakamoto-cho, Nagasaki-shi, Japan

A coenzyme A- and nicotinamide adenine dinucleotide-linked pyruvate dehydrogenase complex has been isolated from pig heart muscle as a multienzyme unit with a molecular weight of approximately 9.0 million.

The pyruvate dehydrogenase complex contains approximately 67 moles of protein-bound lipoic acid and 14 moles of bound flavin adenine dinucleotide. The highly purified complex is free of thiamine pyrophosphate and the activity in the dismutation assay was restored by added thiamine-PP, a Km of 4.2 x 10-6 m.

All preparations of the pyruvate dehydrogenase complex examined showed absolute dependence on added CoA and NAD in the dismutation assay.

Submitted on April 19, 1966


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