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The Fractionation of Immunoglobulins with Insolubilized Concanavalin A
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1972
Year
ImmunohematologyImmunocytochemical TechniqueImmunologyGlycobiologyImmunodominancePeptide ScienceAnalytical UltracentrifugationImmunoassaysProtein PurificationBioanalysisImmunochemistryAutoantibodiesAntibody EngineeringCarbohydrate ContentConcanavalin A-bound IggSummary A MethodChromatographyBiochemistryAutoimmunityInsolubilized Concanavalin AAntibody BiologyNatural SciencesImmunoglobulin EMedicine
Summary A method is described for the facile separation of IgG and IgM based on their differences in carbohydrate content. When a preparation of specific anti-hapten antibody is applied to a column of Sepharose-insolubilized concanavalin A, an unbound fraction containing IgG is washed through the column uncontaminated by other classes of immunoglobulins. The column-bound protein is then eluted with 0.2 M α-methylmannoside. This material contains all the IgM plus about 5% of the original IgG. This concanavalin A-bound IgG appears to be absorbed specifically to the column since reapplication of this material results in the majority of it being rebound, due perhaps to some structural variation in the carbohydrate moieties it contains.