Properties of phosphorylated NADP+-specific glutamate dehydrogenase fromEscherichia coli
β Scribed by Hsiu-Ping P. Lin; Henry C. Reeves
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 851 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0343-8651
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The NADP-specific glutamate dehydrogenase of a high B-lactam producing industrial strain of Penicillium chrysogenum was purified to homogeneity. The enzyme (M, = 339000 f 34000) was demonstrated to have a homohexamer quaternary structure with a subunit molecular mass of M, = 56000 f 2000. The N-term
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
In Saccharomyces cerevisiae, the presence or absence of NADP-specific glutamate dehydrogenase does not affect inhibition of sporulation by ammonia, suggesting that the inhibition is not mediated by this enzyme.