Literature DB >> 1846821

The octapeptide corresponding to the region of the highest homology between alpha-interferon and thymosin-alpha 1 effectively competes with both cytokines for common high-affinity receptors on murine thymocytes.

V P Zav'yalov1, E V Navolotskaya, V M Abramov, V G Galaktionov, I S Isaev, O A Kaurov, A T Kozhich, V A Maiorov, A N Prusakov, R N Vasilenko.   

Abstract

The octapeptide corresponding to human interferon-alpha 2 (Hu IFN-alpha 2) sequence 131-138 has high affinity to murine thymocyte receptors (Kd = 4.2 x 10(-12) M, about 700 receptors per cell). The peptide receptor binding is inhibited by both Hu rIFN-alpha 2 (Ki = 8.6 x 10(-10) M) and thymosin-alpha 1 (TM-alpha 1) (Ki = 3 x 10(-7) M) as well as by the octapeptide homologous to the TM-alpha 1 sequence 16-23 (Ki = 4.5 x 10(-7) M). The peptide from IFN-alpha 2 (131-138) activates murine thymocyte blast transformation at a concentration of 10(-11) M in the presence of 2.5 micrograms/ml of concanavalin A.

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Year:  1991        PMID: 1846821     DOI: 10.1016/0014-5793(91)80113-h

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  1 in total

1.  Protein engineering of de novo protein with predesigned structure and activity.

Authors:  D A Dolgikh; A E Gabrielian; V N Uversky; M P Kirpichnikov
Journal:  Appl Biochem Biotechnol       Date:  1996 Oct-Nov       Impact factor: 2.926

  1 in total

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