title: HPLC chiral stationary phases produced with isolated human serum albumin fragments.
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.
authors.affiliation: Faculty of Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Hyogo, Japan.
authors.forename: Hisami
authors.initials: H
authors.lastname: Matsunaga
authors.forename: Qiang
authors.initials: Q
authors.lastname: Fu
authors.forename: Jun
authors.initials: J
authors.lastname: Haginaka
mesh_terms: D002851:Chromatography, High Pressure Liquid / Q000379:methods; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry*; D004364:Pharmaceutical Preparations / Q000097:blood; D012709:Serum Albumin / Q000737:chemistry* / Q000302:isolation & purification; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013237:Stereoisomerism
chemical_list: D010446:Peptide Fragments; D004364:Pharmaceutical Preparations; D012709:Serum Albumin