| Autor: |
Shafer, Jules A., Chiancone, Emilia, Vittorelli, Letizia M., Spagnuolo, Carla, Mackler, Bruce, Antonini, Eraldo |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 1972, Vol. 31 Issue 1, p166-171, 6p |
| Abstrakt: |
The binding of reduced cofactor (NADH) to glutamate dehydrogenase has been studied by gel filtration, equilibrimn dialysis and fluorescence enhancement. The number of binding sites significantly exceeds 1 per polypeptide chain (1.3 per chain of molecular weight 56 000), the saturation curve gives indications of slight positive interactions. The presence of GTP, glutamate and ADP, apart from increasing the affinity of NADH for glutamate dehydrogenase, appears to affect both the number of binding sites and the cooperativity of the binding. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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