Partial Purification and Characterization of Glucose-6-phosphate Isomerase from Dictyostelium discoideum

Glucose-6-phosphate Dehydrogenase PURIFICATION AND PARTIAL CHARACTERIZATION

Glucose-6-phosphate dehydrogenase has been purified lOOO-fold from pig liver. This enzyme exists as an active dimer of molecular weight 133,000 and an inactive monomer of molecular weight 67,500. The pH of maximum activity is 8.5 and the ionic strength maximum is 0.1 to 0.5 M. Glucose-6-phosphate dehydrogenase is highly specific for NADP+ and glucose B-phosphate. Apparent K, values of 3.6 pM an...

Characterization of Human Glucose - 6 - Phosphate Isomerase of Different Sizes

Galactose-6-phosphate dehydrogenase. Purification and partial characterization.

A new enzyme, galactose-6-phosphate dehydrogenase has been purified about 50-fold from goat liver. The enzyme can be distinguished from the nonspecific hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase by its high substrate specificity and absolute pyridine nucleotide requirement. In contrast to the hexose-6-phosphate dehydrogenase, this enzyme is located exclusively in the...

Cloning and characterization of an anaerobically induced cDNA encoding glucose-6-phosphate isomerase from maize.

Anaerobic stress in maize (Zea mays L.) leads to a drastic alteration in gene expression and results in the selective synthesis of a small number of polypeptides named anaerobic proteins (Sachs et al., 1980). Other plants studied showed similar responses when subjected to an anaerobic environment (Russell et al., 1990). To date, the majority of the anaerobic proteins that have been identified w...

Characterization of RapGAP1 from Dictyostelium discoideum

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