Abstract

An adsorbent gel, Butyl Toyopearl 650-M, is known to adsorb proteins in a given medium with mild hydrophobic interaction. Usability of the adsorbent gel for on-line deproteinization of HPLC analysis was investigated. The samples spiked in serum were some drugs which covered a wide range of hydrophilicity and hydrophobicity. Two methods were employed; one is for hydrophilic compounds by adsorption of protein, and the other for hydrophobic compounds by direct adsorption of analytes on the gel. Both methods gave quantitative recovery of analytes regardless of the protein binding ratio; the relative standard deviation was 0.8-3.3%. However, for a mixture of anticonvulsants with a wide range of hydrophobicity, simultaneous deproteinization and analysis of all components was unsuccessful. This method of deproteinization was especially suitabble for the analysis of hydrophilic compounds in serum.

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