Binding studies of oxovanadium(V) with ovalbumins (OA) |
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| Authors: | S R Verma J P S Arora J S Shankar R Chand |
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| Institution: | 1. Pollution Relevant Research Laboratory, Post-graduate Department of Zoology, D.A.V. College, 251001, Muzaffarnagar, India
2. Department of Chemistry, D.A.V. College, 251001, Muzaffarnagar, India
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| Abstract: | The effect of protein oxovanadium(V) ion concentration and pH on the ratio of diffusion current (id/id0) was studied in vanadium(V) ovalbumin-S and denatured ovalbumin systems. In both the cases marked decrease in diffusion current was observed at the respective pH values, indicating that binding takes place with cationic groups of the proteins. The binding sites (n) were found to be pH dependent. The uniformity of logK and ΔG 0 value at all pH values indicated the involvement of same sites in interaction. Furthermore, the linear scatchard plots in both the systems supported the involvement of single class of independent sites in oxovanadium(V) anion interaction. The difference in binding sites (n) has been attributed to the folded structure of ovalbumin-S while unfolded one of denatured ovalbumin. |
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