Analysis of IgG glycopeptides by alkaline borate gel filtration chromatography.
A protocol for the characterization of IgG glycopeptides is described. Central to this scheme is the novel application of an alkaline borate buffer to gel filtration chromatography. The use of this buffer significantly enhances the resolution of glycopeptides. Furthermore, it results in the separation of a unique size class of glycopeptides derived from IgG secreted by murine hybridomas. Although predominantly neutral, these glycopeptides differ both qualitatively and quantitatively by lectin affinity chromatography from the other glycopeptides which are presumably derived from the Fc portion of IgG.
Rothman
R J
RJ
Wistar Institute of Anatomy and Biology, Philadelphia, PA 19104.
Warren
L
L
D001881:Borates; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D006020:Glycopeptides; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G; D009439:Neuraminidase / Q000378:metabolism; D009844:Oligosaccharides
D001881:Borates; D006020:Glycopeptides; D007074:Immunoglobulin G; D009844:Oligosaccharides; D009439:Neuraminidase