SUCCINIC DEHYDROGENASE IN THE PARTICULATE FRACTION OF MYCOBACTERIUM AVIUM

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Abstract
A cell-free extract from Mycobacterium avium was fractionated into particulate and soluble fractions by differential centrifugation. Succinic dehydrogenase was shown to be loqalized in the particulate fraction. However, reduction of 2,6-dichlorophenolindophenol or cyto-chrome c by succinate using the particulate fraction requires addition of the soluble fraction, which can be replaced satisfactorily by crystalline heart muscle fumarase. Succinic dehydrogenase activity assayed with dye or cytochrome c is quite insensitive to either malonate or oxalacetate. Aerobic oxidation of succinate using the particulate fraction also requires the soluble fraction. The latter fraction cannot be replaced by heart muscle fumarase, but can be replaced partially by oxalacetic decarboxylase from Micrococcus lysodeikticus. It is suggested that this particulate fraction contains a mitochondria-like substance.