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JBC, Vol. 251, Issue 17, 5381-5385, Sep, 1976

Interaction of human interferons with immobilized hydrophobic amino acids and dipeptides

E. Sulkowski, M. W. Davey and W. A. Carter

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.
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				M Rubinstein, S Rubinstein, P. Familletti, M. Gross, R. Miller, A. Waldman, and S Pestka Human leukocyte interferon purified to homogeneity Science, December 22, 1978; 202(4374): 1289 - 1290. [Abstract] [PDF]