Salt influence on glutathione*/Schistosoma japonicum glutathione S-transferase binding
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2003Abstract
There has been some speculation about the salt independence of Schistosoma japonicum glutathione S-transferase (Sj26GST, EC.
2.5.1.18), but this aspect has not been carefully studied before. To establish the basis for a further development of this dependence,
we have performed a methodical study of the influence of some important ions and their concentration on the binding properties of
glutathione to Sj26GST by means of isothermal calorimetry and fluorescence quenching. Salts like NaCl, Na2SO4 and MgSO4 do
not change practically the affinity of the protein for its substrate, whilst MgCl2 has the effect of decreasing the affinity as its
concentration rises. However, the enthalpy change is not affected by all the salts studied, and so, the entropy change is the causal
factor in dropping the affinity. We also looked at the conformational stability of the protein under different conditions to check the
structural changes they provide, and found that the unfolding parameters are pra...
Palabra/s clave
Glutathione S-transferase
Schistosoma japonicum
Glutathione
Unfolding
Fluorescence
Binding
Microcalorimetry