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Abstract
Vanadate(V) anions have been found to modulate the activity of a large number of enzymes. To elucidate these interactions, a physico-chemical study of the binding of meta-vanadate(V) with two typical proteins ovalbumin and transfusion gelatin has been taken up. The binding has been investigated by polarographic method at pHs 7.5 and 9.3, and at 30°C. Values of intrinsic association constant, standard Gibb's free energy change, and the number of amino acids involved in these bindings are reported. Analysis of the binding sites has been done.
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