|Phosphofructokinase from the posterior gills of the euryhaline crab, Eriocheir sinensis: evidence for its regulation by phosphorylation|Benoit, M.-A.; Debauche, P.; Devos, P. (1994). Phosphofructokinase from the posterior gills of the euryhaline crab, Eriocheir sinensis: evidence for its regulation by phosphorylation. J. Comp. Physiol. (B Biochem. Syst. Environ. Physiol.) 164(2): 165-171. dx.doi.org/10.1007/BF00301660
In: Journal of comparative physiology. Part B. Biochemical, systemic, and environmental physiology. Springer: Heidelberg; Berlin. ISSN 0174-1578, more
PHOSPHOFRUCTOKINASE; PROTEIN KINASES; GLYCOLYSE; GILL; CRAB; ERIOCHEIRSINENSIS
|Authors|| || Top |
- Benoit, M.-A.
- Debauche, P.
- Devos, P.
Phosphofructokinase from the posterior gills of the euryhaline crab Eriocheir sinensis acclimated to freshwater is likely regulated in part via phosphorylation induced by endogenous cyclic nucleotide-dependent protein kinases. Phosphofructokinase from gill extracts devoid of low molecular weight compounds by chromatography through a PD10 Sephadex column, incubated in the presence of cAMP or cGMP protein kinases activators (cAMP or cGMP, Mg-ATP and Mg2+), shows an increased catalytic activity. This treatment is accompanied by 32P incorporation into the proteins immunoprecipitated with anti-mammalian phosphofructokinase polyclonal antibodies cross-reacting with the analog crustacean enzyme. Our results indicate that the covalent modification induced by these nucleotide-dependent protein kinases activates the glycolytic enzyme by increasing its affinity for its substrate and, when the activation is specifically due to cAMP-dependent protein kinases, by also reducing the homotropic cooperativity between its multiple substrate binding sites.