Cell surface immunoglobulin. XVI. Polypeptide chain structure of mouse IgM and IgD like molecule

U. Melcher, J. W. Uhr

Research output: Contribution to journalArticlepeer-review

47 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)409-415
Number of pages7
JournalJournal of Immunology
Volume116
Issue number2
StatePublished - Dec 1 1976

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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