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The octapeptide corresponding to the region of the highest homology between α‐interferon and thymosin‐α 1 effectively competes with both cytokines for common high‐affinity receptors on murine thymocytes
Author(s) -
Zav'yalov V.P.,
Navolotskaya E.V.,
Abramov V.M.,
Galaktionov V.G.,
Isaev I.S.,
Kaurov O.A.,
Kozhich A.T.,
Malorov V.A.,
Prusakov A.N.,
Vasilenko R.N.,
Volodina E.Yu.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80113-h
Subject(s) - thymosin , receptor , interferon , homology (biology) , chemistry , biology , microbiology and biotechnology , immunology , biochemistry , amino acid
The octapeptide corresponding to human interferon‐α 2 (Hu IFN‐α 2 ) sequence 131–138 hu??? high affinity to murine thymocyte receptors ( K 6 = 4.2 × 10 −11 M, about 700 receptors per cell). The peptide/receptor binding is inhibited by both Hu rl FN‐α 1 ( K 1 = 8.6 × 10 −10 M) and thymosin‐α 1 (TM‐α 1 ) ( K 1 = 3 × 10 −??? M) as well as by the octapeptide homologous to the TMα‐α 1 sequence 16–23 ( K 1 = 4.5 × 10 −1 M). The peptide from IFN‐α 1 (131–138) activates murine thymocyte blast transformation at a concentration of 10 −11 M in the presence of 2.5 μ/ml of concanavalin A.