[Purification and some properties of electrophoretic variants of 6-phosphogluconate dehydrogenase from rat erythrocytes].
Purification procedure of electrophoretic variants FF and SS of 6-phosphogluconate dehydrogenase (6-PGD) is described. The method includes (NH4)2SO4 fractionation and chromatography on DEAE- and CM-celluloses. Isoenzymes were purified about 5000 fold, and were found to be homogenous by disc electrophoresis in 7% polyacrylamide gel. It was found by comparative studies of activities of variants FF and SS, that pH optimum was 8.2 for variant FF and 8.8 for variant SS. Km for 6-phosphogluconate were found to be 17,5-10(-5) M for variants SS and FF respectively.
D000818:Animals; D004589:Electrophoresis, Disc; D004912:Erythrocytes / Q000201:enzymology*; D014644:Genetic Variation; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000097:blood / Q000302:isolation & purification; D007700:Kinetics; D010734:Phosphogluconate Dehydrogenase / Q000097:blood* / Q000302:isolation & purification; D051381:Rats
D007527:Isoenzymes; D010734:Phosphogluconate Dehydrogenase
Ochistka i nekotorye svoĭstva elektroforeticheskikh variantov 6-fosfogliukonatdegidrogenazy iz eritrotsitov krysy