Tetanus toxoid purification by sephadex G100 and G200 to achieve a high purified toxoid and comparison between toxoid purified by ultra filtra cut off 100 kd.
2008
Mofzali, Fatemeh | Mir Jalili, A`li | Aminiyan, Mahdi | Madani, Rasul | Asli, Esma`il | A`bbasi, Ebrahim | Madani, Farsa | Karimi, Shahla
Sephadex could be purify tetanus toxoid into a non flocculating protein ,slow flocculating protein , rapid flocculating protein and non-protein materials(soluble in 20% trichloroacetic acid). In this Study tetanus toxoid was loaded to sephadex G100 and G200 columns (D2.5 and H130 cm) eluted with saline at 4؛C .Total fractions were collected at flow rate of 0.3 ml/min.Fractions obtained from the column were monitored for UV absorbance's at 280 nm . Total protein content was determined by burette method, titration by flocculation and immunigenisity by and ELISA methods respectively. The results showed that F1 (G100) was flocculating proteinF2 (G100) was no protein. F1 (G200) was non-flocculating protein, F2 (G200) was slow flocculating protein, F3 (G200) was rapid flocculating protein and F4 (G200) was non protein. F3(G200) was found to have a higher purity and even more immunigenisity. The present method may suggest as a good alternative to the traditional method where purification of tetanus toxoid is required. This purification provides a good opportunity to scale the production scheme up or down.
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