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Antiserum raised against riboflavin binding protein purified from peacock (Pavo cristatus), Hen (Gallus gallus) and observed cytotoxic activity on in-vitro cell cultures (HeLa cell lines)

G.Rajender, B.Laxma Reddy, G.Benarjee, M.S.K.Prasad, D.R.Krishna

Riboflavin binding protein (Rfbp)was purified fromPeacock (Pavo cristatus) Egg- white, egg-yolk and Hen (Gallus gallus) egg-white and egg-yolk. Riboflavin binding protein (RfBP) was isolated first time in India frompeacock eggs (Pavo cristatus). The Rfbp was purified in two steps, DEAESephadex A-50 ion exchange chromatography. The final purification of proteins (Rfbp) was achieved on Sephadex G-100.The protein contentwas estimated with Lowry method. The purity of the proteins was judged by cylindrical and slab-gels, SDS-PAGE techniques. These proteins showed a single band on SDS gels and the molecular weight was 29 Kilodaltons. Antiserum was raised against these RfbpÂ’s in rabbit. These proteins are emulsified in FreundÂ’s complete adjuvant and injected subcutaneously at weekly intervals for 4 weeks into the rabbit at multiple sites. The rabbit antiserum was collected through the ear vein, 7 days after the final injection. This serum was analyzed in-vitro method with HeLa cervical cancer cell-ines.MTT[(3-(4,5-dimethylthiazol-2yl)-2,5-diphenyltetrazoliumbromide] measures the metabolic activity of the viable cells. The viable cell counting with trypan blue dye exclusion method. There was more than 85 percent of cell death was observed. The anticancer activity of Riboflavin binding proteins (Rfbp) purified from egg-white of Peacock (Pavo cristatus)94.6%,egg-yolk87.7 and Hen(Gallus gallus)egg-white87.5,eggyolk 86.2%contains anticancer activity on HeLa cell lines.