高速液体クロマトグラフィーによるアンジオテンシンI-変換酵素の迅速定量法
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概要
- 論文の詳細を見る
Activity of angiotensin I-converting enzyme [EC 3.4.15.1] was assayed by chromatographical separation of the synthetic substrate (Bz-Gly-Gly-Gly or Bz-Gly-His-Leu) and the cleaved product (Bz-Gly) using high-speed liquid chromatography (HLC). Bz-Gly from each unhydrolyzed substrate was separated on the column of Zipax SAX (50 cm×2.1 mm i.d.), and with 0.01 M potassium phosphate buffer (pH 6.27) as eluant. In this condition, 1.3×10^<-4> to 2.4×10^<-3> units of the enzyme activity was measurable when Bz-Gly-Gly-Gly was used as the substrate, and 3.3×10^<-4> to 6.0×10^<-3> units of the activity was assayed with Bz-Gly-His-Leu as the substrate.
- 社団法人日本薬学会の論文
- 1978-09-25
著者
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添田 秦司
福岡大学薬学部生化学
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井ノ口 仁一
Faculty Of Pharmaceutical Sciences Fukuoka University
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井ノ口 仁一
福岡大学薬学部
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永松 淳雄
福岡大学薬学部
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添田 秦司
Faculty of Pharmaceutical Sciences, Fukuoka University
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添田 秦司
Faculty Of Pharmaceutical Sciences Fukuoka University
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添田 秦司
福岡大学 薬
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