Purification of Bungarus multicinctus antivenin by affinity chromatography
Related Experiment Video
Updated: Oct 2, 2026

12:16
High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
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.

