PMID: 2509567Nov 13, 1989Paper

Isolation of immunoglobulin G by affinity chromatography using an IgG Fc receptor protein from Streptococcus dysgalactiae coupled to a solid phase

Journal of Immunological Methods
C Lämmler, R Sting

Abstract

A culture of Streptococcus dysgalactiae (C 26) was shown to bind only to 125I-IgG, whereas another S. dysgalactiae culture (C 12) bound both 125I-IgG and 125I-albumin. The IgG-binding proteins could be readily solubilized by lysozyme treatment of the bacteria and isolated by affinity chromatography on IgG Sepharose. The purified IgG-binding protein from S. dysgalactiae C 26, which lacked simultaneous albumin binding activity, precipitated with IgG preparations from man, cow, horse, pig and mouse but not with chicken IgG. This IgG-binding protein was coupled to CNBr-activated Sepharose and subsequently used for the purification of IgG from both bovine and human serum. SDS-PAGE and immunoelectrophoretic studies confirmed the purity of the eluted proteins.

References

Jan 1, 1978·Journal of Immunological Methods·J W Goding
Aug 1, 1988·Scandinavian Journal of Immunology·M YarnallL B Corbeil
Sep 1, 1989·Zentralblatt Für Bakteriologie : International Journal of Medical Microbiology·C Lämmler, C Frede
Jun 10, 1986·Journal of Immunological Methods·C LämmlerH Blobel
Nov 1, 1985·Nihon saikingaku zasshi. Japanese journal of bacteriology·C Sugimoto
Dec 30, 1982·Journal of Immunological Methods·J J Langone

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Citations

Aug 9, 1991·Journal of Immunological Methods·L M LoomesM A Kerr
Oct 1, 1992·Journal of Veterinary Diagnostic Investigation : Official Publication of the American Association of Veterinary Laboratory Diagnosticians, Inc·D A MurphyC Burgos

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