PURIFICATION AND PROPERTIES OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE FROM YEAST ENDOMYCES MAGNUSII

1. By disintegration of mitochondria from Endomyces magnusii using French Press, an ATPase [EC 3.6.1.3] protein was extracted in latent form. The protein was purified by fractionation with polyethyleneglycol-MgSO4 without inducing ATPase activity. The enzyme was highly purified by chromatography on a DEAE-cellulose column, and at the same time its ATPase activity was induced.2. Activation of the latent ATPase, both In solubilized or in particle bound state, was also attained by heat treatment especially in a high concentration of salts. Magnesium ion was partially effective for protecting activation.3. The properties of the yeast ATPase were compared with those of mammalian enzymes. The enzymatic properties of the former resembled those of beef heart enzyme with a few exceptions. © 1969 BY THE JOURNAL OF BIOCHEMISTRY.