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Purification and characterization of NADP-dependent glutamate dehydrogenase from the commercial mushroomAgaricus bisporus

✍ Scribed by J. J. P. Baars; H. J. M. Op den Camp; A. H. A. M. Hoek; C. Drift; L. J. L. D. Griensven; J. Visser; G. D. Vogels

Publisher
Springer
Year
1995
Tongue
English
Weight
727 KB
Volume
30
Category
Article
ISSN
0343-8651

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Purification and properties of the NADP-dependent glutamate dehydrogenase fromDictyostelium discoideum
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NADP-dependent glutamate dehydrogenase from Dictyostelium discoideum was purified 9300 fold with a yield of 4.6%. The enzyme is a hexamer of apparent molecular weight 294 kDa on Sephacryl S400 and a subunit molecular weight of 52 kDa as determined by SDS gel electrophoresis. The apparent Kms for alp