In Vitro Binding Assay of 31Methionine-oxidized Cholecystokinin Octapeptide to the CCKB Receptor
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概要
- 論文の詳細を見る
Methionine (Met) residues of cholecystokinin octapeptide (CCK8) are easily oxidized to produce Met sulfoxide and/or sulfone of CCK8. In order to investigate the effect of modification at Met of CCK8 for its CCKB receptor, we evaluated the binding affinity of 4 oxidized forms of CCK8 for CCKB receptor expressed in the plasma membrane of LoVo cells, by performing a flow cytometry-based competitive binding assay using fluorescein isothiocyanate (FITC)-labeled CCK8. Oxidative modification of CCK8 at 28Met and 31Met caused to increase its binding affinity. The affinity of 31Met sulfone CCK8 was strongest and was significantly higher (by 20-30%) than that of native CCK8 (p<0.05). In contrast, the binding affinity of modified CCK8 was attenuated on replacing 31Met with 31Leu, 31Lys, or 31His.
- 社団法人 日本薬学会の論文
著者
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Ichiba Hideaki
Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
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Yajima Takehiko
Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
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Fukushima Takeshi
Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
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Ichiba Hideaki
東邦大学 薬学部薬品分析学
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Nakamoto Mio
Department of Pharmacy, Ichikawa General Hospital, Tokyo Dental College
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Yajima Takehiko
Department Of Analytical Chemistry Faculty Of Pharmaceutical Sciences Toho University
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Nakamoto Mio
Department of Analytical Chemistry, Faculty of Pharmaceutical Sciences, Toho University
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