Purification and Characterization of a Pregnancy-Associated Protein: TJ6s

Authors

  • M. Mandal,

    1. Department of Microbiology and Immunology, Finch University of Health Sciences/The Chicago Medical School, 3333 Green Bay Road, North Chicago, Illinois
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  • K. D. Beaman Ph.D.

    Corresponding author
    1. Department of Microbiology and Immunology, Finch University of Health Sciences/The Chicago Medical School, 3333 Green Bay Road, North Chicago, Illinois
      Department of Microbiology and Immunology, Finch University of Health Sciences/ The Chicago Medical School, 3333 Green Bay Road, North Chicago, IL 60064.
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Department of Microbiology and Immunology, Finch University of Health Sciences/ The Chicago Medical School, 3333 Green Bay Road, North Chicago, IL 60064.

Abstract

PROBLEM: Characterization of the soluble form of a novel protein, TJ6 (TJ6s) with immune suppressive activity from murine fetoplacental units.

METHOD: Preferential ammonium sulfate precipitation, gel filtration and ion-exchange chromatography were employed to purify the protein TJ6s from murine fetoplacental units using an anti-peptide antibody as a detection tool. Biological activity of the purified protein was studied in lymphocyte proliferation assays.

RESULTS: Purified TJ6s has a Mr of approximately 18 kDa as evidenced by SDS-PAGE in both reducing and non reducing conditions. It exerted a strong anti-proliferative activity in both anti-CD3 and Con A proliferation lymphocyte proliferation assays but not in a PHA assay, suggesting that the anti-proliferative effects on T cells are exerted only on cells specifically activated directly through T cell receptor complex.

CONCLUSION: The results indicate that TJ6s is a novel anti-proliferative protein that has many of the characteristics that are considered necessary for survival of the fetal allograft.

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