Isolation of Phytolacain G and Its Inhibition Measured by Affinity Labeling
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概要
- 論文の詳細を見る
A cysteine protease, phytolacain G, was purified to homogeneity from unripe fruits of pokeweed (Phytolacca americana). The apparent molecular mass of the purified phytolacain G was 25.5kDa. The caseinolytic activity of the enzyme was completely inhibited by a synthetic peptide containing an S-(3-nitro-2-pyridinesulfenyl)group (Npys). The inhibitory activity of this compound against phytolacain G resembled that for papain.
- 社団法人日本農芸化学会の論文
- 1995-09-23
著者
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KANEDA MAKOTO
Department of Pediatrics, Hokkaido University Graduate School of Medicine
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Kaneda M
Department Of Chemistry Faculty Of Science Kagoshima University
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YONEZAWA Hiroo
Department of Chemistry, Faculty of Science, Kagoshima University
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UCHIKOBA Tetsuya
Department of Chemistry, Faculty of Science, Kagoshima University
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YONEZAWA Hiroo
Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kagoshima University
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Hamada Takaaki
Department of Chemistry, Faculty of Science, Kagoshima University
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Matsueda Rei
New Lead Research Laboratories, Sankyo Co., Ltd.
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Kaneda Makoto
Department Of Chemistry Faculty Of Science Kagoshima University
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Matsueda R
Sankyo Co. Ltd. Tokyo Jpn
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Matsueda Rei
New Lead Research Laboratories Sankyo Co. Ltd.
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Yonezawa Hiroo
Laboratory Of Biochemistry Department Of Chemistry Faculty Of Science Kagoshima University
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Hamada T
Department Of Chemistry Faculty Of Science Kagoshima University
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UCHIKOBA Tetsuya
Kagoshima University Musium
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Uchikoba T
Kagoshima University Musium
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Uchikoba Tetsuya
Department Of Chemistry Faculty Of Science Kagoshima University
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