Purification and Properties of Bakers' Yeast Trehalase

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Purification 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 ...

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Purification 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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Purification 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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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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Purification and properties of acetyl coenzyme A synthetase from bakers' yeast.

Acetyl-CoA synthetase, utilized in a coupled reaction system, has been shown to be applicable to the spectrophotometric determination of propionic and methylmalonic acids in biological fluids. The isolation of acetyl-CoA synthetase from yeast is simpler than the purification from mammalian sources. This study also presents some properties of the yeast enzyme and compares it to the more extensiv...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1964

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)91238-x