Stimulation of Mg2+-independent form of Ca2+-ATPase by a low molecular mass protein purified from goat testes cytosol.
Comp Biochem Physiol B Biochem Mol Biol
; 146(1): 131-8, 2007 Jan.
Article
en En
| MEDLINE
| ID: mdl-17126581
ABSTRACT
A low molecular mass protein purified from goat (Capra hircus) testes cytosol following gel filtration and anion exchange chromatographic separation stimulates Mg(2+)-independent Ca(2+)-ATPase activity without any significant effect on Mg(2+)-dependent Ca(2+)-ATPase. Stimulation of the ATPase is due to an increase in the rate of dephosphorylation of the overall reaction step of the enzyme. Binding of the stimulator increases the affinity of Ca(2+)-ATPase for Ca(2+). An analysis of enzyme kinetics reveals a reversible type of binding of the stimulator to the ATPase and non-competitive type of stimulation with respect to the substrate. Stimulation seems due to binding of the protein at a single site following Michaelis-Menten model. The protein can also counter the effect of calcium antagonists exerted on the ATPase. The pI of the protein is 6.2 and its molecular mass has been determined to be 13, 961 by Q-TOF-MS.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Testículo
/
Cabras
/
ATPasas Transportadoras de Calcio
/
Citosol
Límite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B Biochem Mol Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
2007
Tipo del documento:
Article
País de afiliación:
India