Glucose-6-phosphate dehydrogenase: partial characterization of the rat liver and uterine enzymes.
Some properties of rat liver and uterine glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP+ oxidoreductase, EC 1.1.1.49) have been determined. A procedure has been used for the purification of rat liver glucose-6-phosphate dehydrogenase to homogeneity (spec. act. 210-225 units/mg protein) from large amounts of liver (0.5-2 kg) with yields of up to 30%. Uterine glucose-6-phosphate dehydrogenase was obtained by immunoprecipitation methods and the properties of radioactively-labeled forms of this enzyme were then determined. The amino acid composition of the liver enzyme was found to be similar to that for the enzyme from other mammalian tissues. The liver and uterine enzymes have a subunit molecular weight of 57000 and a pI of 6.5. The NH2-terminal amino acid of both enzymes was found to be pyroglutamate.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005260:Female; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification*; D007526:Isoelectric Point; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011761:Pyrrolidonecarboxylic Acid; D051381:Rats; D014599:Uterus / Q000201:enzymology*
D000596:Amino Acids; D005954:Glucosephosphate Dehydrogenase; D011761:Pyrrolidonecarboxylic Acid