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  • Title: In vivo binding of human inter-alpha-trypsin inhibitor free heavy chains to hyaluronic acid.
    Author: Jessen TE, Odum L, Johnsen AH.
    Journal: Biol Chem Hoppe Seyler; 1994 Aug; 375(8):521-6. PubMed ID: 7529027.
    Abstract:
    In vivo binding of human inter-alpha-trypsin inhibitor to hyaluronate was investigated by immunoelectrophoretic techniques. Pathological synovial fluids and follicular fluids both contain high concentrations of soluble hyaluronate. Heavy chain epitopes of inter-alpha-trypsin inhibitor were firmly associated with the hyaluronate in synovial fluid and follicular fluid. The hyaluronate-bound inter-alpha-trypsin inhibitor epitopes did not cross-react immunologically with bikunin. Several hyaluronate-bound inter-alpha-trypsin inhibitor fragments with molecular masses in the range 120,000-30,000 Da were demonstrated by immunoblotting. Heavy chain 1 of inter-alpha-trypsin inhibitor was shown to associate with hyaluronate by amino acid sequence analysis of isolated hyaluronate-bound proteins. These data indicate that in vivo metabolism of inter-alpha-trypsin inhibitor takes place in pathological synovial fluid and in ovarian follicular fluid shortly before ovulation.
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