Abstract
Immunoglobulin production stimulating factor (IPSF) IIα was purified from Namalwa cell lyzate by ammonium sulfate precipitation, hydrophobic interaction chromatography and gel filtration. The purified IPSF was estimated a 106 KD protein which was composed of a polypeptide of 40 KD and two polypeptides of 33KD by gel filtration and SDS polyacrylamide gel electro-phoresis. The 33KD protein extracted from SDS polyacrylamide gel showed IPSF activity, but not the 4 0 KD protein. The IPSF activity was fairly stable in alkaline but unstable in acidic solution. In a serum-free medium, the IPSF-IIα stimulated IgM production of human-human and mouse-mouse hybridomas 4–15 and 2-fold, respectively. However, IgG production of neither human nor mouse was stimulated by the factor in the same serum-free medium.
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 callMore From: Production of Biologicals from Animal Cells in Culture
Disclaimer: 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.
