[81] Binding of human interferons to immobilized albumin

摘要: Publisher Summary Human interferon bind selectively to albumin immobilized on agarose opened up an entirely new field of study the intrinsic hydrophobicity mammalian interferons. The binding human directly agarose, even at high ionic strength, suggests presence nonelectrostatic forces in interaction. In addition its hydrophobic interaction with albumin-agarose, fibroblast displays many other properties consistent hydrophobicity. For example, under physiological solvent conditions, it also binds L-tryptophan, D-tryptophan, L-phenylalanine, and L-tyrosine either cyanogen bromide-activated or via molecular arms. Ethylene glycol is again required eluent for efficient displacement. Studies various straightchain hydrocarbons (molecular arms) when establish a nature binding, (1) length hydrocarbon ligand strength are positively correlated, (2) stronger interactions observed ligands terminated apolar rather than polar head groups, (3) reversal occurs by use solutes.