PMID: 9648230Jul 2, 1998Paper

Rice bifunctional alpha-amylase/subtilisin inhibitor: characterization, localization, and changes in developing and germinating seeds

Bioscience, Biotechnology, and Biochemistry
H YamagataT Iwasaki

Abstract

A bifunctional alpha-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 alpha-amylase from germinating rice seeds weakly. It inhibited rice alpha-amylase more than barley alpha-amylase, and the inhibition of rice alpha-amylase was greater at higher pHs. RASI did not inhibit trypsin, chymotrypsin, cucumisin, or mammalian alpha-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.

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Citations

Nov 16, 2001·Biochemical and Biophysical Research Communications·H Wang, T B Ng
Aug 2, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Yi Hung LinChun Jung Chen
Feb 22, 2002·European Journal of Biochemistry·Octávio L FrancoMaria F Grossi-De-Sá
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Apr 9, 2008·Journal of Chemical Ecology·Biqing SongWenxiong Lin
Jul 7, 2020·Journal of Food Science and Technology·Rakrudee SarnthimaAnupong Joompang
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