High-affinity binding was demonstrated between suppressor-T-cell-derived bioactive glycosylation-inhibiting factor GIF and helper T hybridomas and natural killer cell line cells. However, affinity of rhGIF for the target cells was generated by replacement of Cys in the sequence with Ala or of Asn with Ser or binding of 5-thionitrobenzoic acid to Cys in the molecule. Such mutations and the chemical modification of rhGIF synergistically increased the affinity of GIF molecules for the target cells. The results indicated that receptors on the target cells recognize conformational structures of bioactive GIF.
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