الفهرس | Only 14 pages are availabe for public view |
Abstract The present study was under taken to purify and characterize vitellogenin protein obtained from Nile tilapia fish (Oreochromis niloticus). at spawning season male, female and monosex at six monthes and one year age. The serum samples and the ovaries were used for purification using sepharose 6 B column (100x2.5 cm) at a flow rate of 60 ml/ hr and 10 ml fraction. Elution volume to female serum samples was 90 ml. Molecular weight of vitellogenin was 580 kDa. And SDSPAGE gave positive results appear as two bands, band 1(Vg2) with molecular weight approximately 120 kDa and band 2 (Vg 1) with molecular weight approximately 170 kDa. The liver samples were collected for PCR technique appeared as a partial clone of Vitellogenin gene, gel electrophoresis revealed bands of PCR products with size of approximately 285bp.The sequence length of the PCR product was 289 base. Oreochomis niloticus vitellogenin protein was found to be rich in valine, glycine, isoleucine, leucine and alanine amino acids and poor in phenyl alanine and histidine amino acids. |