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Evaluation of selective competitive binding of basic drugs to α1-acid glycoprotein variants
http://hdl.handle.net/2297/21764
http://hdl.handle.net/2297/217640990d419-5376-4bce-8527-19b2348efba1
| 名前 / ファイル | ライセンス | アクション |
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PH-PR-ISIZAKI-J-95.pdf (201.9 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-04 | |||||
| タイトル | ||||||
| タイトル | Evaluation of selective competitive binding of basic drugs to α1-acid glycoprotein variants | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Ishizaki, Junko
× Ishizaki, Junko× Fukaishi, Akiko× Fukuwa, Chie× Yamazaki, Satoko× Tabata, Mayu× Ishida, Takuya× Suga, Yukio× Arai, Kunizo× Yokogawa, Koichi× Miyamoto, Kenichi |
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| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学医薬保健研究域薬学系 | |||||
| 書誌情報 |
Biological and Pharmaceutical Bulletin 巻 33, 号 1, p. 95-99, 発行日 2010-01-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0918-6158 | |||||
| NCID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA10885497 | |||||
| DOI | ||||||
| 関連タイプ | isIdenticalTo | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1248/bpb.33.95 | |||||
| 出版者 | ||||||
| 出版者 | Pharmaceutical Society of Japan = 日本薬学会 | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | We examined the binding of various basic drugs to the F1S and A genetic variants of α1-acid glycoprotein (AGP), which were isolated from native human commercial AGP (total AGP) by chromatography on an immobilized copper(II) affinity adsorbent. The values of the dissociation constant (Kd) of some basic drugs with the F1S variant in equilibrium dialysis differed characteristically from those with the A variant. The selective binding to these variants was evaluated by measuring the displacement ratio of dicumarol bound to the F1S variant or that of acridine orange bound to the A variant, using circular dichroism spectroscopy. There was reasonably good agreement between the Kd values and displacement ratios. There was a characteristic difference between the values of inhibition constant (Ki) of basic drugs towards dipyridamole binding to F1S and towards disopyramide binding to A in total AGP. We found that the Ki values for dipyridamole binding were well correlated with the Kd values for the F1S variant, whereas those for disopyramide binding were well correlated with the Kd values for the A variant. In conclusion, the higher the affinity of basic drugs for AGP, the more they inhibit the binding of other basic drugs, and further, the inhibitory potency depends on the selectivity of binding to the AGP variants. © 2010 Pharmaceutical Society of Japan. | |||||
| 権利 | ||||||
| 権利情報 | (c) 2010 The Pharmaceutical Society of Japan | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| 関連URI | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://www.jstage.jst.go.jp/article/bpb/33/1/33_95/_article | |||||
