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Immunologic and Immunochemical Studies on the Gar, Lepisosteus Platyrhincus

II. Purification and Characterization of Immunoglobulin¹

From the Department of Microbiology, University of Miami School of Medicine, Miami, Florida and University of Florida, College of Medicine, Gainesville, Florida

Abstract

Purified gar 14S immunoglobulin, obtained by DEAE-cellulose chromatography followed by Sephadex G-200 gel filtration, was found to have a molecular weight of 650,000 and a relatively high hexose content, and to be composed of disulfide-linked H (m.w. 70,000) and L (m.w. 22,000) polypeptide chains present in equimolar amounts. Based upon these data it is proposed that this 14S protein is a tetrameric form of IgM. Immunoelectrophoretic analysis of fractions from Sephadex G-200 with rabbit anti-gar H- and L-chain antisera indicated that this was the only class of immunoglobulin present in gar serum.

Footnotes

¹ This research was supported by United States Public Health Service Research Grant AI-05758 from the National Institute of Allergy and Infectious Diseases.

² Present address: Department of Microbiology, University of Florida College of Medicine, Gainesville, Florida.