HPLC Chiral Stationary Phases Produced with Isolated Human Serum Albumin Fragments.

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  • MATSUNAGA Hisami
    Faculty of Pharmaceutical Sciences, Mukogawa Women’s University
  • FU Qiang
    Faculty of Pharmaceutical Sciences, Mukogawa Women’s University
  • HAGINAKA Jun
    Faculty of Pharmaceutical Sciences, Mukogawa Women’s University

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Abstract

The enantioselectivity of HPLC chiral stationary phases produced with human serum albumin (HSA) fragments was investigated. An HSA fragment (HSA-FG75) was isolated by size-exclusion chromatography following peptic digestion of HSA. The isolated HSA-FG75 was mainly an N-terminal half peptide with an average molecular weight of about 35000 daltons. The HSA and HSA-FG75 proteins were bound to aminopropylsilica gels activated by N,N′-disuccinimidyl carbonate. Though the HSA-FG75 column showed lower enantioselectivities for all of the racemates tested than the intact HSA column, the enantioseparations of the racemates tested were attained with a shorter analysis time on the HSA-FG75 column. These results are ascribable to removal of the non-specific binding sites of HSA, changes in the globular structure of the HSA fragment and/or changes in the local environment around the binding sites. Further, the HSA-FG75 column was as stable as the intact HSA column for repetitive injection of samples.

Journal

  • Analytical Sciences

    Analytical Sciences 18 (1), 27-30, 2002

    The Japan Society for Analytical Chemistry

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