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• W2018711478 abstract "We examined the biochemical and structural properties of oryzacystatin-II, a phytocystatin in rice (Oryza sativa L. japonica), under heat-stress conditions. The enzyme inhibitory reactivity of oryzacystatin-II was enhanced by heating in a temperature-dependent manner and reached a maximum level by heating at 65 °C for 10 min. Size-exclusion chromatography showed that oryzacystatin-II forms a homodimer at ambient temperature and that the enhancement of inhibitory reactivity is due to the conversion of the dimeric to a monomeric form. The monomeric form of oryzacystatin-II reverted to the dimer during storage at 4 °C, suggesting that dimerization is an intrinsic property of oryzacystatin-II. The affinity of the monomer for cysteine proteinases was significantly higher than that of the dimer. This is the first paper to describe the noncovalent dimerization for a cystatin under nonstress conditions. Keywords: Oryzacystatin-II; cystatin; dimerization; cysteine proteinase inhibitor" @default.
• W2018711478 created "2016-06-24" @default.
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• W2018711478 date "2007-02-13" @default.
• W2018711478 modified "2023-10-16" @default.
• W2018711478 title "Oryzacystatin-II, a Cystatin from Rice (<i>Oryza sativa</i> L. <i>japonica</i>), Is a Dimeric Protein: Possible Involvement of the Interconversion between Dimer and Monomer in the Regulation of the Reactivity of Oryzacystatin-II" @default.
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• W2018711478 doi "https://doi.org/10.1021/jf062637t" @default.
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