Optimum pH Control Mechanism for Porcine Pancreatic α-Amylase
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概要
- 論文の詳細を見る
We studied the substrate-dependence of pH activity of porcine pancreatic α-amylase by using a series of p-nitrophenyl malto-oligosaccharides. The mechanism controlling the optimum pH of mammalian α-amylase involved the reception and recognition of a substrate component at some other substrate binding sites, in addition to those at subsite 5 that were reported previously [K. Ishikawa et al., Biochemistry, 32, 6259-6265 (1993)].
- 社団法人日本農芸化学会の論文
- 1995-06-23
著者
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Ishikawa Kazuhiko
National Institute of Bioscience and Human-Technology
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Matsui Ikuo
National Institute of Bioscience and Human-Technology
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Ishikawa Kazuhiko
Natl. Inst. Of Biosci. And Human-tech.
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Matsui Ikuo
Natl. Inst. Of Tech. And Evaluation
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Ishikawa Kazuhiko
National Inst. Advanced Industrial Sci. And Technol. Osaka Jpn
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HONDA Koichi
National Chemical Laboratory for Industry
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Ishikawa K
National Inst. Advanced Industrial Sci. And Technol. Osaka Jpn
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Matsui I
National Inst. Biosci. And Human‐technol. Ibaraki
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Honda K
Kyoto Univ. Kyoto Jpn
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Ishikawa Kazuhiko
National Chemical Laboratory For Industry
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Matsui Ikuo
National Chemical Laboratory for Industry
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