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Purification and Characterization of a Pregnancy‐Associated Protein: TJ6s
Author(s) -
Mandal M.,
Beaman K. D.
Publication year - 1995
Publication title -
american journal of reproductive immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.071
H-Index - 97
eISSN - 1600-0897
pISSN - 1046-7408
DOI - 10.1111/j.1600-0897.1995.tb01139.x
Subject(s) - ammonium sulfate precipitation , size exclusion chromatography , antibody , lymphocyte , biology , receptor , immune system , microbiology and biotechnology , chemistry , biochemistry , immunology , enzyme
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.