## Abstract The effect of various salts on the enzymatic activity of beefβliver glutamate dehydrogenase, on the binary enzymeβreduced coenzyme (NADH or NADPH) comples, as well as on the ternary complex with glutamate was investigated in aqueous solution (0.067__M__ phosphate buffer, pH 7.6). Bindin
Studies on the effect of nacl on the activity of Eriocheir sinensis glutamate dehydrogenase
β Scribed by R. Gilles
- Publisher
- Elsevier Science
- Year
- 1974
- Tongue
- English
- Weight
- 581 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0020-711X
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## Abstract The viscosity of bovine liver glutamate dehydrogenase solutions was studied at 10 and 20Β° C in 0.2.__M__ sodium phosphate buffer at pH 7, in the concentration range 0.1β8 mg/ml. A method for the study of the viscosity of very dilute solutions of associating enzymes is described. It was
## Abstract In the active site of lactate dehydrogenase important roles are given to aminoacids His195 and Arg171. The coenzyme nicotinamide adenine dinucleotide (NAD) is required in oxidized form (NAD^+^) for the enzymatic oxidation of the substrate __L__βlactate. Molecular orbital methods CNDO/2,