CRYSTALLINE ALCOHOL DEHYDROGENASE FROM BAKERS' YEAST
نویسندگان
چکیده
منابع مشابه
Formaldehyde dehydrogenase from bakers' yeast.
In the course of studies of formaldehyde metabolism in yeast (I), an enzyme was found that catalyzed the oxidation of formaldehyde in the presence of glutathione and diphosphopyridine nucleotide. A similar enzyme was discovered independently by Strittmatter and Ball in liver (2). This paper describes the partial purification and some of the properties of yeast formaldehyde dehydrogenase. Some e...
متن کاملProtein kinase activity in commercially available crystalline yeast alcohol dehydrogenase.
Commercially available crystalline yeast alcohol dehydrogenase contained protein kinase activity. Casein and phosvitin were readily phosphorylated, but whole calf thymus histone was not. The protein kinase activity was inhibited by KCl, was not stimulated by cyclic AMP and could be separated from the alcohol dehydrogenase activity by sucrose density centrifugation.
متن کاملDNA polymerases from bakers' yeast.
Two DNA polymerases are present in extracts of commercial bakers' yeast and wild type Saccharomyces cerevisiae grown aerobically to late log phase. Yeast DNA polymerase I and yeast DNA polymerase II can be separated by DEAE-cellulose, hydroxylapatite, and denatured DNA-cellulose chromatography from the postmitochondrial supernatants of yeast lysates. The yeast polymerases are both of high molec...
متن کاملThe preparation and properties of crystalline alcohol dehydrogenase from liver.
Kinetic studies of alcohol dehydrogenase prepared from horse liver by different methods have given different results (Theorell, Nygaard & Bonnichsen, 1955; Dalziel, 1958; Theorell, 1958; K. Dalziel, unpublished work, 1957). The most active crystalline preparations have been obtained by a modification of earlier methods (Bonnichsen, 1950; Bonnichsen & Brink, 1955) in which the principal new feat...
متن کاملYeast Alcohol Dehydrogenase : Molecular Weight
The alcohol dehydrogenases (ADH) crystallized from yeast (1, 2) and from horse liver (3) differ in many of their properties. The mammalian enzyme forms a complex with reduced diphosphopyridine nucleotide in which the absorption band of the coenzyme at 340 rnp is shifted to 325 rnh (4). This permitted the direct study by Theorell and Chance (5) of the stoichiometry and dissociation constant of t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1950
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)51151-6