title: Interaction of human interferons with immobilized hydrophobic amino acids and dipeptides.
abstract: Human fibroblast interferon binds to L-tryptophan, D-tryptophan, L-phenylalanine, and L-tyrosine, all immobilized directly to cyanogen bromide-activated agarose, as well as to L-tryptophan and D-tryptophan methyl ester, both immobilized via molecular arms. The retention of fibroblast interferon is selective and results in a 2300-fold purification. Human leukocyte interferon binds neither to L-tryptophan attached directly to an agarose matrix nor to L-tryptophan immobilized via a molecular arm; it binds, however, to immobilized L-tryptophyl-L-tryptophan and L-tryptophyl-L-tryrosine. When retained, both interferons cannot be displaced unless ethylene glycol is included in the eluant, indicating a hydrophobic interaction. The interaction takes place under physiologic solvent conditions, thus revealing the high intrinsic hydrophobicity of both interferons.
mesh_terms: D000596:Amino Acids; D001665:Binding Sites; D002846:Chromatography, Affinity; D004151:Dipeptides; D005347:Fibroblasts; D006801:Humans; D007372:Interferons / Q000302:isolation & purification; D007962:Leukocytes; D011485:Protein Binding
chemical_list: D000596:Amino Acids; D004151:Dipeptides; D007372:Interferons