Abstract
Purification of the surface antigen of Paramecium tetraurelia (termed i-antigen) by previously published procedures has been shown to result in preparations which frequently contain contaminating proteins including a thiol-activated protease. Alternate procedures for the purification of i-antigen were developed using ion-exchange chromatography. While certain of these procedures result in a homogeneous preparation of i-antigen, the poor yields obtained make these procedures impractical. An alternate method for the purification of i-antigen was developed using immunoaffinity chromatography. Purification by this technique proved to be superior to the various standard procedures described previously. The immunoaffinity column is rapid and results in a recovery, on the average, of over 95% of the applied material. The columns are readily regenerated and may be used numerous times without loss of capacity or purification ability. The i-antigen purified by this method appears homogeneous immunologically and electrophoretically on polyacrylamide gel electrophoresis and isoelectric focusing.
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.
