The aim of this study was to purify glucose-6-phosphate dehydrogenase (G6PD) from domestic goat (Capra aegagrus hircus) erythrocytes and to investigate its some in vitro kinetic properties. Blood was taken on ACD-A solution and erythrocytes were purified, and then they were hemolysated. In the study DEAE-cellulose as anion and CM-Sephadex as cation exchange column chromatographic and ammonium sulphate precipitation and dialysis methods were used. G6PD was purified 45000 fold in a yield of 23%. Molecular weight was found 210000 by Sephadex G-200. Four subunits of this enzyme were found 52000 Km and Vmax values for G6PD were determined as 3.34 x 10-4 M and 642 mm/min. IN addition we found that levels of Mg2+from 1 x 10-3 M to 6 x 10-3 M are increasing activity of G6PD and 10-4 M dehydroepiandrosterone is preventing whole activity of G6PD.
M K CAYCI ,K M KHAN ,V BAYAZIT ,
You can use below filter to find your desired issue