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Interaction of a synthetic peptide of the interferon α‐2 C‐terminal part with human blood leukocytes
Author(s) -
Danilkovitch A.V.,
Kharitonenkov A.I.,
Freze K.V.,
Shevalier A.F.,
Kolosova O.V.,
Bulargina T.V.,
Kirkin A.F.,
Gusev M.V.
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)81387-n
Subject(s) - peptide , human blood , cholera toxin , peptide sequence , chemistry , biological activity , interferon , sequence (biology) , amino acid , biochemistry , binding site , microbiology and biotechnology , biology , in vitro , immunology , endocrinology , gene , physiology
A biologically active synthetic peptide, 2438, representing the 124–138 amino acid sequence of the human interferon α‐2 (IFN α‐2) molecule, which is known to possess IFN‐like antiproliferative activity, specifically binds to human blood leukocytes. Scatchard plots reveal two different K fd values, for the ‘low’ and ‘high’ affinity binding. The interaction of the 125 I‐labelled peptide 2438 with the cells is not impaired by human IFN α‐2 or cholera toxin.