Year-end Sale % OFF 
Abstract
An IgG Fc-binding protein was isolated from alkaline extracts of group A streptococci type 15 by ion-exchange chromatography and immunosorption on an IgG column. Ample use of protease inhibitors was necessary to achieve successful isolation. 600 micrograms protein was obtained from 60 g bacteria (wet weight). The protein appeared homogeneous on agarose gel and sodium dodecyl sulfate polyacrylamide gel electrophoresis and had an apparent molecular weight of 29,500. It contained appreciable amounts of the amino acids glutamic acid, alanine, leucine, aspartic acid and lysine, but little or no tyrosine, phenylalanine, proline, glucosamine or galactosamine. It precipitated human monoclonal IgG of all four sub-classes in agarose gels as well as polyclonal IgG, IgG Fc and normal human serum. It did not precipitate IgG Fab, IgA, IgM, IgD or free kappa or lambda chains.
Published Version
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: International archives of allergy and applied immunology
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.
