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hemodialysis/oryza sativa
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Interaction of rice (Oryza sativa) lectin with N-acetylglucosaminides. Fluorescence studies.
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The interaction of lectin isolated from rice (Oryza sativa) embryos with N-acetylglucosaminides was studied by equilibrium dialysis and fluorescence. Equilibrium dialysis with 4-methylumbelliferyl-(GlcNac)2 showed that rice lectin (Mr 38000) contains four equivalent saccharide-binding sites.
Inactivation of alcohol dehydrogenase in rice seedlings is related to a microsomal fatty acid alpha-oxidation system.
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The selective inactivation of alcohol dehydrogenase by the inactivator found in the microsomal fraction of rice (Oryza sativa) seedlings growing in air (Shimomura, S. & Beevers, H. (1983) Plant Physiol. 71, 736-741; 742-746) was further studied. This inactivation was found to be essentially
Small-scale interaction of iron and phosphorus in flooded soils with rice growth.
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In the rhizosphere of flooded paddy soils, the solubilization, efflux, and uptake of phosphorus (P) are highly intertwined with iron (Fe) redox cycling. However, the direct observation of Fe-P coupling in the rhizosphere is challenging. This study combined high-resolution dialysis (HR-Peeper) and
Refolding and purification of recombinant OsNifU1A domain II that was expressed by Escherichia coli.
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OsNifU1A is a NifU-like rice (Oryza sativa) protein, discovered recently. Its amino acid sequence is very homologous to the sequence of cyanobacterial CnfU and to the sequences of NifU C-terminal domains. Based on its sequence, OsNifU1A is probably a modular structure consisting of two CnfU-like
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