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Purification and characterization of NADP+-specific glutamate dehydrogenase fromEscherichia coli

โœ Scribed by Hsiu-Ping P. Lin; Henry C. Reeves


Publisher
Springer
Year
1991
Tongue
English
Weight
469 KB
Volume
22
Category
Article
ISSN
0343-8651

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Purification and properties of the NADP-
โœ F. Pamula; J. F. Wheldrake ๐Ÿ“‚ Article ๐Ÿ“… 1991 ๐Ÿ› Springer ๐ŸŒ English โš– 523 KB

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