Abstract
Human IgG separated by Cohn fractionation showed variability in the content of aggregates, plasminogen and anticomplement activity. The plasminogen was removed or markedly reduced by affinity chromatography on Sepharose-lysine. Anticomplement activity was reduced by chromatography of Cohn fraction II on DEAE-cellulose. Preparations of IgG obtained by chromatography of intermediates from Cohn fractionation (e.g. Cohn FII + FIII or FII + FIII W) on DEAE-cellulose were devoid of aggregates, plasminogen and exhibited reduced anticomplement activity. The initial levels of specific antibody activity to viral agents were recovered in the IgG fractions. Fragmentation of IgG during storage was prevented or greatly reduced by removal of plasminogen by affinity chromatography on Sepharose-lysine.
Sign-in/Register to access full text options 
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.
