作者: Yutaka Sadakane , Hisami Matsunaga , Kazuya Nakagomi , Yasumaru Hatanaka , Jun Haginaka
DOI: 10.1016/S0006-291X(02)00716-7
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摘要: Abstract Ovoglycoprotein from chicken egg whites (OGCHI) has been used as a chiral selector to separate drug enantiomers. However, neither the amino acid sequence of OGCHI nor responsible part for recognition (protein domain or sugar moiety) yet be determined. First, we isolated cDNA clone encoding OGCHI, and clarified which consists 203 acids including predictable signal peptide 20 acids. The mature shows 31–32% identities rabbit human α1-acid glycoproteins (α1-AGPs). Thus, should α1-AGP. Second, recombinant α1-AGP was prepared by Escherichia coli expression system, its ability confirmed capillary electrophoresis. Since proteins expressed in E. are not modified any moieties, this result that protein is recognition.