Purification and Characterization of Chymotrypsin-like Proteinase from Euphausia superba
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概要
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Proteinase A2, a chymotrypsin type enzyme, was purified about 280-fold from an extract of Euphausia superba by DEAE-cellulose column chromatography, gel filtration on Sephadex G-75, and hydroxyapatite column chromatography. The final preparation was electrophoretically homogeneous. The molecular weight was 29, 000. The optimum pH was 8.0 and the optimum temperature was 45°C. Proteinase A2 hydrolyzed casein but not benzoyl-DL-arginine-p-nitroanilide, unlike other serine proteinases from antarctic krill.1) This enzyme was inhibited by DFP, PMSF, soybean trypsin inhibitor, but not TLCK, leupeptin, or antipain. Proteinase A2 could hydrolyze benzoyl-tyrosineethylester and was inhibited by chymostatin. These results suggest that proteinase A2 from antarctic krill seemed to be a new type of anionic chymotrypsin.
著者
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Kimoto Koichi
Department Of Clinical Nutrition Tokyo Kasei University
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Murakami Kazuo
Institute Of Applied Biochemistry University Of Tsukuba
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Yokoi Toshihiro
Department Of Neurosurgery Tenri Hospital
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YOKOI Toshihiro
Department of Nutrition, Tokyo Kasei University
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MURAKAMI Kazuo
Institute of Applied Biochemistry, the University of Tsukuba
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