Abstract
The interactions of human serum albumin (HSA) with a poly(vinyl alcohol) gel packing (Asahipak GS-520) for high-performance liquid chromatography of proteins were investigated. Under certain conditions, the elution of HSA from the GS-520 column was retarded and its chromatogram was split into two peaks, indicating weak adsorption of HSA onto the gels and also the existence of two subfractions, i.e. human mercapto-albumin (HMA) and human non-mercapto-albumin (HNA). The chromatograms were confirmed to be greatly influenced by the salt composition, the pH, and the temperature of the isocratic mobile phase. It is characteristic for the adsorption of HSA onto the gels to be suppressed at a pH near its isoelectric point. The HSA-gel interaction parameters calculated using an adsorption chromatography theory demonstrate that the adsorption of HSA is caused by enthalpy-driven interactions, which are depressed by lowering the pH, in addition to hydrophobic interactions. Under the recommended chromatographic conditions for high resolution of HMA/HNA, it was found that the HSA samples possessed some subfractions besides HMA and HNA fractions.
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