Distinct Ig H chains in a primitive vertebrate, Eptatretus stouti

Peter J. Hanley, Ian M. Seppelt, Andrew A. Gooley, Jeffrey W. Hook, Robert L. Raison*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    20 Citations (Scopus)

    Abstract

    Serum Ig from the Pacific hagfish, Eptatretus stouti, was isolated by affinity chromatography using a specific mAb (H.45). Analysis of the ∼210-kDa molecule by SDS-PAGE under reducing conditions revealed two H chains of ∼77 KDa (H1) and ∼70 kDa (H2) and L chains of ∼30 kDa. H1 and H2 were shown to differ with respect to their peptide maps, amino-terminal amino acid sequences, and reactivity to the mAb H.45, suggesting that they represent discrete H chain isotypes. Two-dimensional nonreducing/reducing SDS-PAGE demonstrated that H and L chains were covalently linked predominantly as H-H-L and H-L configurations. Noncovalently bound L chains were also found. H-H-L complexes were shown to contain H1-H2 heterodimers of H chains in addition to H1-H1 homodimers.

    Original languageEnglish
    Pages (from-to)3823-3828
    Number of pages6
    JournalJournal of Immunology
    Volume145
    Issue number11
    Publication statusPublished - 1 Dec 1990

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