HPLC chiral stationary phases produced with isolated human serum albumin fragments. |
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Authors: | Hisami Matsunaga Qiang Fu Jun Haginaka |
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Institution: | Faculty of Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Hyogo, Japan. |
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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 35,000 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. |
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