Binding of synthetic LKEKK peptide to human T-lymphocytes
- Authors: Navolotskaya E.V.1, Zinchenko D.V.1, Zolotarev Y.A.2, Kolobov A.A.3, Lipkin V.M.1
-
Affiliations:
- Branch of Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
- Institute of Molecular Genetics
- State Research Institute of Highly Pure Biopreparations
- Issue: Vol 81, No 8 (2016)
- Pages: 871-875
- Section: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/150979
- DOI: https://doi.org/10.1134/S0006297916080071
- ID: 150979
Cite item
Abstract
The synthetic peptide LKEKK corresponding to sequence 16-20 of human thymosin-α1 and 131-135 of human interferon-α2 was labeled with tritium to specific activity 28 Ci/mol. The [3H]LKEKK bound with high affinity (Kd = 3.7 ± 0.3 nM) to donor blood T-lymphocytes. Treatment of cells with trypsin or proteinase K did not abolish [3H]LKEKK binding, suggesting the non-protein nature of the peptide receptor. The binding was inhibited by thymosin-α1, interferon-α2, and cholera toxin B subunit (Ki = 2.0 ± 0.3, 2.2 ± 0.2, and 3.6 ± 0.3 nM, respectively). Using [3H]LKEKK, we demonstrated the existence of a non-protein receptor common for thymosin-α1, interferon-α2, and cholera toxin B-subunit on donor blood T-lymphocytes.
Keywords
About the authors
E. V. Navolotskaya
Branch of Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Author for correspondence.
Email: navolotskaya@ibch.ru
Russian Federation, Pushchino, Moscow Region, 142290
D. V. Zinchenko
Branch of Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: navolotskaya@ibch.ru
Russian Federation, Pushchino, Moscow Region, 142290
Y. A. Zolotarev
Institute of Molecular Genetics
Email: navolotskaya@ibch.ru
Russian Federation, Moscow, 123182
A. A. Kolobov
State Research Institute of Highly Pure Biopreparations
Email: navolotskaya@ibch.ru
Russian Federation, St. Petersburg, 197110
V. M. Lipkin
Branch of Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
Email: navolotskaya@ibch.ru
Russian Federation, Pushchino, Moscow Region, 142290