Author/Authors :
da Silva e Mouta Junior، نويسنده , , Sergio and Otلvio Alves Vianna، نويسنده , , Carlos and Ennes، نويسنده , , Ilka and de Andrade Gomes، نويسنده , , Selma and da Silva Freire، نويسنده , , Marcos and Domingos da Silva، نويسنده , , Edimilson and Giovanni De Simone، نويسنده , , Salvatore and Terezinha Baroni de Moraes، نويسنده , , Marcia، نويسنده ,
Abstract :
Purification of recombinant hepatitis B surface antigen (recHBsAg) produced in a stable Chinese hamster ovary (CHO) cell line was evaluated using Linx Affinity Purification System (Invitrogen, USA). To purify HBsAg secreted by this cell line, a murine monoclonal antibody (MAbAH1) raised against native HBsAg was used. The purified AH1MAb was conjugated with phenyldiboronic acid (PDBA) and immobilized on the immunoaffinity chromatographic support. Using an optimized protocol the affinity column was able to purify recHBsAg from supernatant of mammalian cells cultures with more than 80% purity. This method showed to be simple and quicker than the current ultracentrifugation methods. The method is also efficient and economical in obtaining purified recHBsAg.
