Journal article Open Access
P. Koteshwar Rao*, G. Rajender
Riboflavin binding protein (Rfbp) was purified from different avian eggs including Pea cock (Pavo cristatus) Egg- white and Hen (Gallus gallus) egg- white Riboflavin binding protein (RfBP) was isolated. The Rfbp was purified in two steps; DEAE-SephadexA-50 ion exchange chromatography. The final purification of proteins (Rfbp) was achieved on SephadexG100.The protein content was estimated with Lowry method. The purity of the proteins was judged by two methods like cylindrical and slab-gels, SDS- PAGE techniques. These proteins showed a single band on SDS gels and the molecular weight was 29 Kilo Daltons. Antiserum was raised against these Rfbp is in rabbit. These proteins are emulsified in Freund is complete adjuvant and injected subcutaneously at weekly intervals for 4 weeks in to the rabbit at multi places. The rabbit anti serum was collected through the ear vein, 7 days after the booster injection. This serum was analyzed in- vitro method with HeLacervical cancer cell- lines. MTT [(3- (4, 5- dimethyl thiazol-2yl)-2, 5-diphenyl tetrazolium bromide] 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 anti cancer activity of Riboflavin binding proteins (Rfbp) purified from egg-white of Pea cock (Pavo cristatus) 87.7% and Hen (Gallusgallus) egg-white 87.5, egg-yolk 86.2% and Emu egg white (Struthio camelus) 85.0 contains anti cancer activity on HeLacelllines.