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Binding of 125 I‐labelled human αinterferon to human lymphoid cells
Author(s) -
Mogensen Knud Erik,
Bandu MarieThérèse,
Vignaux Franloise,
Aguet Michel,
Gresser Ion
Publication year - 1981
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910280508
Subject(s) - interferon , raji cell , microbiology and biotechnology , cell culture , biology , binding site , dissociation constant , alpha interferon , receptor , interferon gamma , interferon alfa , in vitro , chemistry , biochemistry , immunology , genetics
To investigate the binding of interferon to human lymphoid cells, we purified human α interferon and radio‐labelled it with iodine −125. Binding at 4°C could be saturated and was inhibited by unlabelled interferon; it was specific for cells of human origin. Dissociation constants for the complex of interferon and receptor site were of the order 10 −9 –10 −11 M. All human cells tested showed such binding. Occupation of these high‐affinity sites, at 37°C, was compared with the inhibition of cellular growth due to interferon. The most sensitive cell line (Daudi) gave a complete biological response with only a fraction of its sites occupied. Evidence of two sites was found for a line (P3HRI) showing intermediate sensitivity. A relatively insensitive line (Raji) showed no response when all its high‐affinity sites were occupied.