Interaction of vanadium(V) oxoanions with ovalbumin and transfusion gelatin

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 degrees 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.