Isolation of HBsAg by immunoaffinity chromatography using the anti-idiotype antibody as an eluting agent.

摘要

A immunoaffinity method for purification of Hepatitis B surface antigen (HBsAg) using monoclonal anti-idiotype (anti-Id) as a specific eluent, is described. Ammonium sulfate fractions of Hepatitis B surface antigen (HBsAg) containing plasma were adsorbed on monoclonal idiotype (Id) immunoadsorbents. Bound material was eluted from the column with the anti-Id of HBsAg. The eluate, contaminating anti-Id, was further purified by gel filtration. The procedure yielded highly purified HBsAg. The final HBsAg Product was free from contaminating humen plasma and mouse ascite proteins. The procedure is generally applicable and particularly attractive when the antigen is unstable in commonly used eluting conditions.