Abstract
Purified hepatitis B surface antigen (HBsAg) of subtype ay was solubilized in guanidinium chloride and submitted to chormatography on Sepharose 4B in the presence of guanidinium chloride. The polypeptides P1 ( M r = 24,000) and P2 ( M r = 29,000) were eluted in the same fraction with a minor contaminant ( M r = 40,000). Large amounts of these two polypeptides were obtained in a single step. This technique which constitutes a method for large-scale purification of the P1 and P2 polypeptides should permit more complete characterization of the P1 and P2 polypeptides and of their antigenic determinants.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
