Rice Bifunctional α-Amylase/Subtilisin Inhibitor : Characterization, Localization, and Changes in Developing and Germinating Seeds
スポンサーリンク
概要
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A bifunctional α-amylase/subtilisin inhibitor (RASI) was purified to electrophoretic homogeneity from rice (Oryza sativa L.) bran. Its molecular mass was 21 kDa by SDS-PAGE and its isoelectric point was 9.05. Purified RASI inhibited subtilisin Carlsberg strongly and inhibited α-amylase from germinating rice seeds weakly. It inhibited rice α-amylase more than barley α-amylase, and the inhibition of rice α-amylase was greater at higher pHs. RASI did not inhibit trypsin, chymotrypsin, cucumisin, or mammalian α-amylase. The RASI was in the outermost part of the rice grain and its subcellular site seemed to be aleurone particles in aleurone cells. SDS-PAGE and western blotting showed that RASI was synthesized in the late milky stage in developing seeds, and it remained fairly constant during the first 7 days of germination.
- 社団法人日本農芸化学会の論文
- 1998-05-23
著者
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IWASAKI Teruo
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University
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Kamasaka Hiroshi
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University
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Yamagata Hiroshi
Laboratory Of Biological Chemistry Faculty Of Agriculture Kobe University
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Yamagata Hiroshi
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University
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KUNIMATSU Kiyoshi
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University
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KURAMOTO Takeshi
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University
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Iwasaki Teruo
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University:(present Address)hagoromo Gakuen J
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Iwasaki Teruo
Laboratory Of Biochemistly Faculty Of Agriculture Kobe University
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Kuramoto Takeshi
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University
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Kunimatsu Kiyoshi
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University
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YAMAGATA Hiroshi
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University
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