Purification and properties of NAD-dependent D-glucose dehydrogenase produced by alkalophilic Corynebacterium sp. No. 93-1.

Purification and Properties of D-glucose-~-phosphate Dehydrogenase*

n-Glucose-6-phosphate dehydrogenase (Zwischenferment) was discovered by Warburg and Christian in 1931 (1, 2). An active preparation was obtained then from horse erythrocytes and in 1932 from the Lebedev juice made from brewers’ yeast (3). Because of its extreme specificity, this enzyme has become an important analytical tool. Various preparations of it have been described, the first being those...

Purification and properties of d-glucose-6-phosphate dehydrogenase.

n-Glucose-6-phosphate dehydrogenase (Zwischenferment) was discovered by Warburg and Christian in 1931 (1, 2). An active preparation was obtained then from horse erythrocytes and in 1932 from the Lebedev juice made from brewers’ yeast (3). Because of its extreme specificity, this enzyme has become an important analytical tool. Various preparations of it have been described, the first being those...

Purification and properties of the phospho and dephospho forms of yeast NAD-dependent glutamate dehydrogenase.

Purification of NAD-dependent mannitol dehydrogenase from celery suspension cultures.

Mannitol dehydrogenase, a mannitol:mannose 1-oxidoreductase, constitutes the first enzymatic step in the catabolism of mannitol in nonphotosynthetic tissues of celery (Apium graveolens L.). Endogenous regulation on the enzyme activity in response to environmental cues is critical in modulating tissue concentration of mannitol, which, importantly, contribute to stress tolerance of celery. The en...

Affinity Purification and Characterization of Recombinant Bacillus sphaericus Phenylalanine Dehydrogenase Produced by pET Expression Vector System

Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 (DE3). The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Re...