title: Hydrophobic interaction of human, mouse, and rabbit interferons with immobilized hydrocarbons.
abstract: Interferons of human, mouse, and rabbit origin bind to straight chain hydrocarbons immobilized on agarose. The hydrophobic nature of binding is established by the following observations: (a) a positive correlation between the length of hydrocarbon ligand and the strength of interaction; (b) a stronger interaction with hydrocarbon ligands terminated with apolar rather than polar head groups; (c) a lack of dependence of binding on ionic strength and pH of the solvent; (d) a reversal of binding by ethylene glycol, a hydrophobic solute; (e) an increasing eluting efficacy of tetraalkylammonium ions with the length of their alkyl substituents. The hydrophobic interactions of human interferon underlie the efficiency of two-step chromatographic procedures. For example, human embryo kidney interferon can be purified about 3,600-fold by sequential chromatography on (a) concanavalin A-agarose, (b) octyl-agarose. Another two-step procedure: (a) concanavalin A-agarose, (b) L-tryptophan-agarose, gives about 10,000-fold purification. The overall recovery of interferon in both cases in close to 90%.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D003208:Concanavalin A; D006801:Humans; D006838:Hydrocarbons; D007372:Interferons / Q000302:isolation & purification; D007668:Kidney; D008297:Male; D051379:Mice; D009928:Organ Specificity; D011817:Rabbits; D012685:Sepharose; D012867:Skin; D013045:Species Specificity
chemical_list: D006838:Hydrocarbons; D003208:Concanavalin A; D007372:Interferons; D012685:Sepharose