title: Glycosylation of polyclonal and paraprotein IgG in multiple myeloma.
abstract: It has previously been shown that in multiple myeloma (MM) each IgG paraprotein exhibits a unique oligosaccharide profile. It has been assumed that this results from a clone specific glycosylation machinery. However, the abnormal physiological environment of the bone marrow in this disease may also affect normal plasma cells producing polyclonal IgG. We present data to show that this is so and that, in two cases, the oligosaccharide profile of the polyclonal IgG reflected that of the paraprotein from the same patient rather than that of normal polyclonal IgG.
authors.affiliation: Department of Immunology, The Medical School, Edgbaston, Birmingham, UK.
authors.forename: M
authors.initials: M
authors.lastname: Farooq
authors.forename: N
authors.initials: N
authors.lastname: Takahashi
authors.forename: H
authors.initials: H
authors.lastname: Arrol
authors.forename: M
authors.initials: M
authors.lastname: Drayson
authors.forename: R
authors.initials: R
authors.lastname: Jefferis
mesh_terms: D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D007074:Immunoglobulin G / Q000097:blood* / Q000737:chemistry / Q000145:classification; D009101:Multiple Myeloma / Q000097:blood*; D009844:Oligosaccharides / Q000032:analysis
chemical_list: D007074:Immunoglobulin G; D009844:Oligosaccharides