Cytochrome aa3 was purified 35to 40-fold from submitochondrial particles of commercial bakers’ yeast. The purification procedure involved solubilization of the enzyme with cholate, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose in the presence of Triton x-100. The purified, active enzyme contained approximately 10 nmoles of heme a per mg of protein and was free of oth...

Massive necrosis of the liver occurs in rats restricted to diets in which yeast is the sole source of protein."' The present report considers the cardiac and hepatic lesions that developed in mice fed diets in which British yeast was the source of protein. In addition, studies have been made of the possible protective actions of dietary supplements (cystine or a-tocopherol) and of the substitut...

ATP is the universal energy substance of all living cells. F1F0-ATP synthase, a multisubunit enzyme found in bacteria, chloroplasts and mitochondria, is responsible for the synthesis of ATP and thus provides energy to almost all living cells. Our research is focused on the mitochondrial complex (mtATPase) of bakers’ yeast Saccharomyces cerevisiae (Fig. 1). Yeast provides a powerful system in wh...

Nicotine adenine dinucleotide-linked primary alcohol dehydrogenase and a newly discovered secondary alcohol dehydrogenase coexist in most strains of methanol-grown yeasts. Alcohol dehydrogenases from methanol-grown yeasts oxidize (--)-2-butanol preferentially over its (+) enantiomorph. This is substantially different from alcohol dehydrogenases from bakers' yeast and horse liver.

Octanoic acid inhibited ethanolic fermentation by Saccharomyces cerevisiae (bakers yeast) and the trehalose accumulation, however did not affect the endogenous degradation of trehalose. This inhibition may be explained by the binding of octanoic acid to hexokinase or other proteins of plasma membrane because they are not necessary for endogenous fermentation. The degradation of trehalose may be...

Aerobically grown bakers’ yeast has been shown to contain two different lactic cytochrome c reductases, one of which is specific for L( +)-lactate (1) and the other of which is specific for D( -)-lactate (2). Neither of these two enzymes is present in anaerobically grown yeast, which contains instead a D( -)lactic dehydrogenase that does not reduce cytochrome c. No L( +)-lactic dehydrogenase is...