Sulkowski E, Davey M W, Carter W A
J Biol Chem. 1976 Sep 10;251(17):5381-5.
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.
人成纤维细胞干扰素能与直接固定在溴化氰活化琼脂糖上的L-色氨酸、D-色氨酸、L-苯丙氨酸和L-酪氨酸结合，也能与通过分子臂固定的L-色氨酸甲酯和D-色氨酸甲酯结合。成纤维细胞干扰素的保留具有选择性，可实现2300倍的纯化。人白细胞干扰素既不与直接连接在琼脂糖基质上的L-色氨酸结合，也不与通过分子臂固定的L-色氨酸结合；然而，它能与固定化的L-色氨酰-L-色氨酸和L-色氨酰-L-酪氨酸结合。当两种干扰素被保留时，除非洗脱液中含有乙二醇，否则它们都不能被置换，这表明存在疏水相互作用。这种相互作用在生理溶剂条件下发生，从而揭示了两种干扰素都具有很高的内在疏水性。
