Dog Pancreatic Arginine Esterases : spontaneously activated on DEAE-Sephadex
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概要
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Tremendous activation of arginine esterases or trypsin-like enzymes from the dog pancreas was observed during DEAE-Sephadex A-50 chromatography of the pancreatic kallikrein. The esterase activity freshly assayed was 7.5 μmoles N^α-benzoyl-L-arginine ethyl ester (BAEE)/min per gram of the pancreas. The enzymes were separated into two fractions by Ampholine isoelectric focusing, their isoelectric points being 4.6 and 4.8. The two esterases purified showed the specific activities with 4.4-7.4 μmoles BAEE/min/A_<280> and 20-36 μmoles N^α-p-toluenesulfonyl-L-arginine methyl ester (TAME)/min/A_<280>, and hydrolyzed N^α-benzoyl-DL-arginine-p-nitroanilide (BApNA) and casein. The esterases were strongly inhibited by Trasylol, soybean trypsin inhibitor, kallikrein inhibitors from potatoes, etc. From chemical and enzymatic properties, both esterases seemed to be anionic trypsins of the dog pancreas.
- 公益社団法人日本薬学会の論文
- 1975-01-25
著者
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守屋 寛
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tok
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法島 義男
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tok
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法島 義男
Faculty Of Pharmaceutical Sciences Science University Of Tokyo:(present Address)department Of Immuno
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山下 円
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tok
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山下 円
Laboratory Of Physiological Chemistry Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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