PMID: 6982069Aug 31, 1982Paper

Activity of synthetic thymosin alpha 1 C-terminal peptides in the azathioprine E-rosette inhibition assay

Biochemistry
T L CiardelliC Birr

Abstract

The helical C-terminal portion of the thymic hormone thymosin alpha 1 exhibits immunological activities in several in vitro assays. The C-terminal region spanning positions 17-28 was subdivided into 11 overlapping peptide segments to collect further information on the molecular signal hypothesis for T lymphocyte differentiation by thymosin alpha 1 derived peptides. All peptides were synthesized by classical means and tested in the azathioprine E-rosette inhibition assay. The results provided additional evidence that a basic-acidic-lipophilic sequence character is a possibly essential feature of a molecular signal for T cell differentiation. Five to seven structures beginning N terminally with lysine fitted this functional key. They showed immunological in vitro activities similar to and even better than the parent hormone thymosin alpha 1 in the ability to express in immature spleen cells from adult thymectomized mice the E-receptor sensitive to azathioprine inhibition.

References

May 1, 1979·Angewandte Chemie·C Birr, U Stollenwerk
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Feb 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·P BurtonA White
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Citations

Feb 25, 1983·Journal of Immunological Methods·K OhgaR A Good
May 1, 1986·Journal of Immunological Methods·G S IncefyB W Erickson
Sep 1, 1988·Annales De L'Institut Pasteur. Immunology·P DuboisL Pereira da Silva
Jan 1, 1987·Immunopharmacology and Immunotoxicology·L DenesL Kisfaludy
Jan 1, 1985·Critical Reviews in Oncology/hematology·R S Schulof

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