Purification of Bungarus multicinctus antivenin by affinity chromatography.

Abstract

Bungarus multicinctus horse antivenin was purified by ammonium sulfate fractionation, gel filtration on Sephadex G-200 column, and affinity chromatography. The specific neutralizing capacity of the antibody preparations showed 2.21-fold, 3.12-fold, and 29.6-fold higher than that of the crude antivenin, respectively.