Resum
An analysis of the molecular properties of the major alcohol dehydrogenase
(E.C.1.1.1.1) allozyme variants found segregating in natural populations of
D. mehnogaster is presented. Our results indicate: (1) ADH-S enzyme has
generally lower Michaelis-Menten constants than those of ADH-F; (2) ADH-S
and ADH-F enzymes display opposite interactions for both co-factor and substrate; and (3) higher levels of ADH are associated with the Adh-fast genotype.
The possible adaptive significance of these findings is discussed.
(E.C.1.1.1.1) allozyme variants found segregating in natural populations of
D. mehnogaster is presented. Our results indicate: (1) ADH-S enzyme has
generally lower Michaelis-Menten constants than those of ADH-F; (2) ADH-S
and ADH-F enzymes display opposite interactions for both co-factor and substrate; and (3) higher levels of ADH are associated with the Adh-fast genotype.
The possible adaptive significance of these findings is discussed.
| Idioma original | Anglès |
|---|---|
| Pàgines (de-a) | 1013-1022 |
| Nombre de pàgines | 10 |
| Revista | Genetics |
| Volum | 95 |
| Estat de la publicació | Publicada - d’ag. 1980 |