Aminopeptidase P, Capable of Hydrolyzing Oligoproline, from Bovine Brain
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概要
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An aminopeptidase P, capable of hydrolyzing oligoproline, was isolated from the homogenate of bovine brain. The molecular mass of the enzyme was 140kDa by gel filtration. The enzyme was activated by Mn^<2+> and inhibited by o-phenanthroline. The enzyme hydrolyzed substrates such as Pro-Pro-Pro-Pro, Pro-Pro-Pro, and Pro-Pro to proline, and cleaved N-terminal amino acids from pep-tides containing penultimate prolines such as bradykinin and neuro-peptide Y.
- 社団法人日本農芸化学会の論文
- 1994-11-23
著者
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Maeda H
Tsukuba R&d Center Fuji Oil Co Ltd.
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Maeda H
Division Of Agronomy And Horticultural Science Graduate School Of Agriculture Kyoto University
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Maeda Hirokazu
Protein Development Dept. Ii Hannan R&d Center Fuji Oil Co.ltd.
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Kobayashi Tsutomu
Institute for Materials Research, Tohoku University
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Maruyama Susumu
National Institute Of Bioscience And Human Technology Agency Of Industrial Science And Technology
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Maruyama Susumu
National Institute Of Bioscience And Human-technology Agency Of Industrial Science And Technology
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Tanaka Hideoki
National Institute Of Bioscience And Human-technology Agency Of Industrial Science And Technology
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Ohmori Takashi
Department of Health and Dietary Science, Research and Development Center, Nippon Meat Packers, Inc.
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Maeda Hidekatu
National Institute of Bioscience and Human-Technology, Agency of Industrial Science and Technology
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Ohmori Takashi
Department Of Health And Dietary Science Research And Development Center Nippon Meat Packers Inc.
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Ohmori Takashi
Department Of Agricultural Chemistry College Of Agriculture And Veterinary Medicine Nihon University
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Kobayashi Tsutomu
Institute For Materials Research Tohoku University
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Kobayashi Tsutomu
Institute Of Applied Biochemistry University Of Tsukuba
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