Isolation of Crystalline Phosphoglucose Isomerase from Brewers' Yeast

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Isolation of Crystalline Phosphoglucose Isomerase from Brewers' Yeast.

In a program to elucidate the mechanism by which phosphoglucose isomerasel participates in the catalyzed isomerization between glucose 6-phosphate and fructose g-phosphate, isolation of the enzyme from several sources is pursued as the basis for quantitative studies of its protein nature. The comparative investigation of several heteroenzymes appears to be a valuable tool in identifying the str...

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The 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...

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Phosphoglucose Isomerase from Human Erythrocyte

Phosphoglucose isomerase (D-glucose 6-phosphate ketol isomerase, EC 5.3.1.9) of the human erythrocyte was resolved into a major and two minor components. The major enzyme form, isomerase a, was purified to constant specific activity and appeared homogeneous bjl chromatography, electrophoresis, and ultracentrifugation. The minor enzyme forms, isomerases b and c, were also prepared in high purity...

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Physical and chemical properties of yeast phosphoglucose isomerase isoenzymes.

Three isoenzymes of brewers’ yeast phosphoglucose isomerase which can be resolved by column chromatography on DEAE-cellulose (NAKAGAWA, Y., AND NOLTMANN, E. A. (1967) J. Biol. Chem. 242, 47824788) have been subjected to physical and chemical characterization. In contrast to the pseudoisoenzymes of rabbit muscle phosphoglucose isomerase (BLACKEWRN, M. N., CHIRGWIN J., M. JAMJZS, G. T., KEMPE, T....

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Subunit and peptide compositions of yeast phosphoglucose isomerase isoenzymes.

Three isoenzymes of yeast phosphoglucose isomerase were studied by physical and chemical methods to establish their subunit properties and to identify the structural differences among them which give rise to their heterogeneous chromatographic behavior. Equilibrium sedimentation ultracentrifugation in 6 M guanidine hydrochloride and polyacrylamide gel electrophoresis in the presence of sodium d...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1965

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)97398-9