Purification and Subunit Structure of Glutathione Reductase from Bakers' Yeast
نویسندگان
چکیده
منابع مشابه
Glutathione reductase from bakers' yeast and beef liver.
The reduction of glutathione by a heat-labile system in liver was discovered by Hopkins and Elliott (1). Later Mann (2) obtained a soluble enzyme preparation from liver which required, for the reduction process, a cofactor and glucose as hydrogen donor. Meldrum and Tarr (3) found that oxidized glutathione was reduced by rat blood and by yeast and demonstrated the function of TPNl as a cofactor ...
متن کاملThe subunit structure of phosphoglucose isomerase from bakers' yeast.
Bakers' yeast phosphoglucose isomerase was studied by both chemical and physical methods to determine its submit structure. Gel filtration in 6 M guanidine HCl as well as acrylamide gel electrophoresis of sodium dodecyl sulfatedentured phosphoglucose isomerase showed two speices corresponding to one-half and one-fourth of the preparative molecular weight of 119,400 determined by equilibrium cen...
متن کاملPurification and Properties of Bakers' Yeast Trehalase.
Since recent surveys of insect hemolymph (1, 2) have shown that trehalose is the major blood sugar, the hydrolytic enzyme trehalase has also awakened the interest of investigators. A purified preparation of the enzyme from Galleria mellonella (3) and from Phormia regina (4) was recently obtained and some of its properties described. The biosynthesis of trehalose with an enzyme preparation from ...
متن کاملPurification and Properties of the Catalase of Bakers’ Yeast
Catalase from bakers’ yeast has been purified to homogeneity in the analytical ultracentrifuge and in gel electrophoresis; sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide gel electrophoresis revealed dissociation of a major component of molecular weight 61,000, which constituted 90% of the total protein of the stain...
متن کاملPurification and properties of the catalase of bakers' yeast.
Catalase from bakers’ yeast has been purified to homogeneity in the analytical ultracentrifuge and in gel electrophoresis; sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide gel electrophoresis revealed dissociation of a major component of molecular weight 61,000, which constituted 90% of the total protein of the stain...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)81737-4