Some properties of the nadp+dependent isocitrate dehydrogenase of rat and pig ovary
✍ Scribed by Patricia M. Stevenson; Janice C. Parker; P.Helen Pearce; Ann V. Ghisalberti; Deborah J. Norman; John W. Sadleir; Peter A. Naumoff; Geraldine Lee
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 778 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0020-711X
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
An NADP+-specific isocitrate dehydrogenase has been purified and characterized from Rhizobium meliloti. The enzyme showed Mn++ or Mg++ requirement. The apparent Km values were 2.00 x 10(-5) M and 1.51 x 10(-5) M for DL-isocitrate and NADP+, respectively. The enzyme was inhibited by ATP, to a lesser
## Abstract The metabolic function of NAD(P)‐glycohydrolase in the streptomycyin‐producing __Streptomyces griseus__ was investigated. Phospho‐adenosinediphospho‐ribose, the product of NAD(P)‐glycohydrolase reaction was shown to interfere as a competitive inhibitor not only with the glucose‐6‐phosph
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