The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum: purification and properties.
作者： F. Pamula , J.F. Wheldrake
DOI: 10.1016/0003-9861(91)90127-5
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摘要: Abstract The NAD-dependent glutamate dehydrogenase (GDH) from Dictyostelium discoideum was purified 1101-fold with a yield of 23.4%. enzyme has an apparent M r 356 kDa, determined using Sephacryl S400, and subunit molecular weight 54 kDa on SDS-polyacrylamide gel electrophoresis. K m s for α-ketoglutarate, NADH, NH 4 + are 0.36 ± 0.03 , 16.0 ±0.1 μ 34.5 2.7 respectively. pH optimum 7.25–7.5. At 0.1 ADP AMP stimulate GDH activity 25 102%, Halfmaximal in the presence is reached at 2.3 71.4 5.5 27.9 3.6
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