Über die Oxydation der Milchsäure und der β-Oxybuttersäure durch den Herzmuskel.

Abstract

CH3CHOHCOOH was oxidized reversibly to CH2COCOOH by coenzyme-activated dehydrogenase of pig heart muscle. These acids, dehydrogenase and co-enzyme formed a thermodynamically reversible oxidation system with EO-181 mv. CH3CHOHCH2COOH was reversibly dehydrogenated to CH3COCH5COOH. The dehydrogenation of CH3CHOHCOOH and of CH3CHOHCH2COOH was activated by the same co-enzyme. The dehydrogenase was highly specific. Aside from these 2 acids, fructose diphosphate is the only substance upon which the enzyme has been found to act, and the same coenzyme is required. The latter appeared to promote only the dehydrogenation and not the reverse action, since this proceeded at the same rate regardless of the presence or absence of coenzyme.