Equilibrium cooperative binding of calcium and protons by sarcoplasmic reticulum ATPase.
AUTOR(ES)
Hill, T L
RESUMO
The cooperative equilibrium binding of Ca2+ by sarcoplasmic reticulum ATPase, as modulated by pH, is analyzed by statistical mechanical treatment of a theoretical model. The model consists of four equivalent subunits, in the form of a square, with nearest-neighbor interactions. Each subunit has one site for binding of one Ca2+ or one proton, but not both. Binding of either ligand on a subunit induces a conformational change in the subunit that alters its interaction with its two neighbors. The model gives good agreement with experimental binding data. It should prove useful as a starting point in the analysis of steady-state ATPase activity as a function of Ca2+ and H+ concentrations.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=346559Documentos Relacionados
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