Carbohydrate as covalent crosslink in human inter-alpha-trypsin inhibitor: a novel plasma protein structure

T E Jessen, K L Faarvang, M Ploug

    74 Citations (Scopus)

    Abstract

    The primary structure of inter-alpha-trypsin inhibitor is partially elucidated, but controversy about the construction of the polypeptide backbone still exists. We present evidence suggesting that inter-alpha-trypsin inhibitor represents a novel plasma protein structure with two separate polypeptide chains covalently crosslinked only by carbohydrate (chondroitin sulphate).

    Original languageEnglish
    JournalFEBS Letters
    Volume230
    Issue number1-2
    Pages (from-to)195-200
    Number of pages6
    ISSN0014-5793
    Publication statusPublished - 28 Mar 1988

    Keywords

    • Alpha-Globulins
    • Amino Acid Sequence
    • Carbohydrates
    • Chondroitin Lyases
    • Chondroitin Sulfates
    • Chromatography, Gel
    • Electrophoresis, Polyacrylamide Gel
    • Humans
    • Hyaluronoglucosaminidase
    • Immunoelectrophoresis
    • Immunosorbent Techniques
    • Molecular Sequence Data
    • Molecular Weight
    • Trypsin Inhibitors
    • Journal Article

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