Colorimetric Measurement of Angiotensin I-Converting Enzyme Activity Using Bilirubin Oxidase-Catalyzed Oxidative Decarboxylation
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概要
- 論文の詳細を見る
A simple colorimetric method for determining the activity of angiotensin I-converting enzyme (ACE) was developed. The assay method is based on the following series of reactions : ACE hydrolyzes a tripeptide substrate, N-benzoyl-L-2-(4-hydroxyphenyl)glycyl-L-histidyl-_L-leucine to liberate N-benzoyl L-2-(4-hydroxyphenyl)glycine. The compound is then converted into 4-hydroxybenzaldehyde (HBA) through oxidative decarboxylation catalyzed by bilirubin oxIdase from Myrothecium verrucaria. Finally, HBA is measured colorimetrically by treatment with 2,4-dinitrophenylhydrazine to evaluate the activity of ACE. The optimum pH of ACE for the substrate was 8.3,and the K_m value aws 0.072mM. The formation rate of HBA was proportional to the ACE concentration, and the correlation coefficient was 0.997.
- 社団法人日本生物工学会の論文
- 1994-01-25
著者
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SHIN Takashi
Department of Applied Microbial Technology, The Kumamoto Institute of Technology
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CHIBA Hiroyuki
Process Development Laboratories, Mercian Corporation
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AGEMATU Hitosi
Central Research Laboratories, Mercian Corporation
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Chiba Hiroyuki
Central Research Laboratories Mercian Corporation
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Shin T
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Shin Takashi
Department Of Applied Microbial Technology Kumamoto Institute Of Technology
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Agematu Hitosi
Central Research Laboratories Mercian Corporation
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Yoshioka Takeo
Central Research Laboratories Mercian Corporation
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Shibamoto Norio
Central Research Laboratories Mercian Co.
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Chiba Hiroyuki
Process Development Laboratories Mercian Corporation
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Agematu Hitosi
Central Research Laboratories Mercian Co.
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Agematu H
Mercian Corp. Fujisawa Jpn
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Takenisi Shigeyuki
Osaka Municipal Technical Research Institute
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Yoshioka Takeo
Central Research Laboratories, Mercian Corporation
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SHIN Takashi
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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