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The Journal of Immunology, 1972, 109: 1402-1404.
Copyright © 1972 by The American Association of Immunologists, Inc.

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The Fractionation of Immunoglobulins with Insolubilized Concanavalin A

Yacob Weinstein1, David Givol and Paul H. Strausbauch2

From the Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel

Abstract

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 {alpha}-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.

Footnotes

1 Address correspondence to Yacob Weinstein, Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel.

2 Recipient of an American Cancer Society postdoctoral fellowship. Present address: University of Miami School of Medicine, Miami, Florida.







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