Purification and Properties of the L-Cysteinyl Ribonucleic Acid Synthetase of Bakers' Yeast
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چکیده
منابع مشابه
Purification and properties of the L-cysteinyl ribonucleic acid synthetase of bakers' yeast.
In this report a method is described for the puritication of the L-cystemyl-RNA synthetase of Bakers’ yeast. The enzyme, which was purified approximately 710-fold, was shown to have a molecular weight of approximately 160,000, and did not contain activity for any of the ammo acids commonly occurring in protein except L-cysteine. Optimum conditions for enzyme activity, such as substrate concentr...
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Lysyl transfer ribonucleic acid synthetase (L-lysine: tRNA ligase (AMP), EC 6.1.1.6) was pursed to a state of apparent homogeneity from bakers’ yeast. For each of two different preparation procedures, a 250to 500-fold purikation of the enzyme was obtained, and the final purification step yielded two distinct protein components with specific activity values of approximately 0.5 and 1.0 pmole of ...
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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 ...
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The mechanism by which an aminoacyl ribonucleic acid synthetase recognizes its transfer ribonucleic acid substrate constitutes one of the central problems in biochemical genetics. Obviously this problem cannot be solved without a thorough understanding of the structure of both enzyme and substrate. Although work on the structure of tRNAr has yielded signal results during the last few years (l-3...
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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: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93115-7