Purification and Characterization of a Pregnancy-Associated Protein: TJ6s
Article first published online: 9 MAY 2013
American Journal of Reproductive Immunology
Volume 33, Issue 1, pages 60–67, January 1995
How to Cite
Mandal, M. and Beaman, K. D. (1995), Purification and Characterization of a Pregnancy-Associated Protein: TJ6s. American Journal of Reproductive Immunology, 33: 60–67. doi: 10.1111/j.1600-0897.1995.tb01139.x
- Issue published online: 9 MAY 2013
- Article first published online: 9 MAY 2013
- Accepted September 29, 1994
- suppressive factor;
- murine fetoplacental unit;
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.