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Cell Surface Immunoglobulin

XVI. Polypeptide Chain Structure of Mouse IgM and IgD-like Molecule¹

From the Department of Microbiology, University of Texas Southwestern Medical School, Dallas, Texas 75235

Abstract

¹²⁵I-membrane IgM, ¹²⁵I-membrane IgD-like molecules, and their constituent chains from iodinated murine splenocytes were characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The apparent m.w. of the heavy chains decreased as the acrylamide concentration was raised. The membrane µ-chain had a slower mobility than did µ-chain from secreted IgM. Unreduced IgM and IgD-like molecules had mobilities consistent with an H₂L₂ structure. Intact IgD-like molecules were replaced after overnight dialysis by molecules with the properties of HL. Unreduced surface IgM had a slower mobility than that of monomeric IgM obtained by partial reduction of secreted IgM.

Footnotes

¹ This work was supported by National Institutes of Health Grants AI1185 and AI10967 and by a National Institutes of Health Postdoctoral Fellowship GM55567 to Ulrich Melcher.

² Present address: Department of Biochemistry, Oklahoma State University, Stillwater, Oklahoma 74074.

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