STUDIES ON GLUCOSE DEHYDROGENASE. II
1954 Volume 41 Issue 1 Pages 67-80
Details
1954 Volume 41 Issue 1 Pages 67-80
1. The purification of glucose dehydrogenase from fresh bovine liver has been described. D-Xylose, L-xylose, and Na gluconate were oxidized at a slower rate than D-glucose by this purified preparation.
2. It was found that glucose dehydrogenase_??_ is inhibited by quinonoids, nitrogen mustard, Cu++, Ag+, urethan, catechin and tea-leaves extract, but not by NaF, D-ascorbic acid, cyanide, other metal ions than Cu++ and Ag+ ions, several sugars such as fructose, galactose, D-xylose, L-xylose, arabinose, quercitol, sucrose, and _??_mannitol, nor by any such SH-reagents as maleic acid, AsO3, oxidized glutathione, sodium iodoacetate, or by several other reagents.
3. It was ascertained by paperchromatographic technique that the primary oxidation product of glucose by liver glucose dehydrogenase is gluconic acid.
4. Although it appears that the glucose dehydrogenase system does not link directly with oxalacetic decarboxylase system, a small amount of oxalacetate was detected only in the co-existence of malate. But the mechanism of this phenomenon is unknown.
