Primary structure of the immunoglobulin J chain from the mouse

G. M. Cann, A. Zaritsky, M. E. Koshland

Research output: Contribution to journalArticlepeer-review

53 Scopus citations

Abstract

The primary structure of the murine J chain was investigated by sequence analysis of the J chain cDNA inserts from two independently cloned chimeric plasmids. The sequence data showed that the two cDNA inserts accounted for all but approximately 100 5' nucleotides of the J chain mRNA and the J chain mRNA encodes a prepeptide of at least 23 amino acids, a mature protein of 137 residues, and an untranslated 3' region of 707 nucleotides exclusive of the 3' poly(A) tract. The amino acid sequence deduced for the mature mouse J chain was found to be 74% identical with that previously determined for the human J chain. By analyzing the conserved features of the sequence, a two-domain structure was generated for the J chain which correlates well with its functions in the polymerization of IgM and IgA. Moreover, by comparing the homologies of the J and heavy chains in mouse and man, evidence was obtained that the structures involved in polymerization are the most conserved elements of immunoglobulin molecules.

Original languageEnglish
Pages (from-to)6656-6660
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number21 I
DOIs
StatePublished - 1 Jan 1982
Externally publishedYes

ASJC Scopus subject areas

  • General

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