glutelin/oryza sativa

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Possible cleavage sites of glutelin partial degradation confirmed by immunological analysis in globulin-less mutants of rice (Oryza sativa L.).

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Proteolytic cleavage or partial degradation of proteins is one of the important post-translational modifications for various biological processes, but it is difficult to analyze. Previously, we demonstrated that some subunits of the major rice (Oryza sativa L.) seed storage protein glutelin are

Variations in glutelin and high molecular weight endosperm proteins among subspecies of rice (Oryza sativa L.) detected by two-dimensional gel electrophoresis.

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Variations in endosperm polypeptides among 16 cultivars of rice were analyzed by two-dimensional gel electrophoresis. One glutelin alpha-subunit (alpha 8) with a molecular mass of 32.5 kDa was exclusively present in indica cultivars. By contrast, the glutelin alpha 3 subunit, with a molecular mass

Evaluation of the quality of a high-resistant starch and low-glutelin rice (Oryza sativa L.) generated through CRISPR/Cas9-mediated targeted mutagenesis

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A high-resistant starch (RS) and low-glutelin diet is beneficial for the health of patients with diabetes and kidney diseases. Rice is an important food crop worldwide. Previous studies demonstrated that downregulating the expression of rice starch branching enzyme IIb (SBEIIb) affected the

A rice (Oryza sativa L.) mutant having a low content of glutelin and a high content of prolamine.

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Among the mutant lines of rice that have been selected for morphological characters, one line, NM67, was found to have a low content of glutelin and a higher content of prolamine in its seed protein than other Japanese cultivars. This mutant is a semi-dwarf and partially sterile line, and its leaves

Capillary electrophoresis for analysis of microheterogeneous glutelin subunits in rice (Oryza sativa L.).

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Glutelin, the major storage protein of rice seed, consists of microheterogenous subunits and partially exists in a macromolecular form that is polymerized by intersubunit disulfide bonds. In order to analyze the glutelin subunits using high-throughput CE, we first identified a sample preparation

Structural homology between semidwarfism-related proteins and glutelin seed protein in rice (Oryza sativa L.).

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Two semidwarfism-related proteins, SRP-1 and SRP-2, were detected as major spots in a long-culm rice cultivar, Norin 29 and its semidwarf near-isogenic line, SC-TN1, respectively, by two-dimensional gel electrophoresis (2D-PAGE). The testcross showed that SRP-1 and SRP-2 are controlled by codominant

Glutelin subtype-dependent protein localization in rice grain evidenced by immunodetection analyses.

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GluA and GluB-4/5 glutelin subfamilies are mainly localized to outer region of the endosperm, particularly in its ventral side, in rice grain, but GluC is localized to throughout the endosperm. The major seed storage protein in rice (Oryza sativa) is glutelin, which forms a vacuole-derived protein

Structural Relationship among the Rice Glutelin Polypeptides.

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When the glutelin protein fraction of rice (Oryza sativa L.) seeds was fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, three size classes of proteins, 51 kilodaltons (kD), 34 to 37 kD, and 21 to 22 kD, as well as a contaminating prolamine polypeptide of 14 kD were

Changes in grain size and grain storage protein of rice (Oryza Sativa L.) in response to elevated UV-B radiation under outdoor conditions.

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Variation in growth, grain size and grain storage protein content of rice (Oryza sativa L.) in response to elevated UV-B radiation under sunlight was examined in a cool rice-growing region of Miyagi Prefecture, Japan, in 1999, 2001 and 2002. Tiller number, dry mass, panicle number, grain yield and

Identification of 4-mercapto-4-methylpentan-2-one as the characteristic aroma of sake made from low-glutelin rice.

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The grassy characteristic aroma perceived in brewed sake made from low-glutelin rice (Oryza sativa L. Mizuhonoka) was examined by gas chromatography-olfactometry and gas chromatography-mass spectrometry. By comparing the odor properties and Kovats retention indices to those of standard compounds,

Expression pattern and activity of six glutelin gene promoters in transgenic rice.

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The shortage of strong endosperm-specific expression promoters for driving the expression of recombinant protein genes in cereal endosperm is a major limitation in obtaining the required level and pattern of expression. Six promoters of seed storage glutelin genes (GluA-1, GluA-2, GluA-3, GluB-3,

Structure and expression of the rice glutelin multigene family.

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A near full-length cDNA and three genomic clones for rice (Oryza sativa L.) glutelin were isolated and studied. Based on nucleic acid sequence and Southern blot analyses, the three isolated glutelin genomic clones were representative members of three gene subfamilies each containing five to eight

RiceRBP: a database of experimentally identified RNA-binding proteins in Oryza sativa L.

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RNA-binding proteins play critical roles at multiple steps during gene expression, including mRNA transport and translation. mRNA transport is particularly important in rice (Oryza sativa L.) in order to ensure the proper localization of the prolamine and glutelin seed storage proteins. However,

Accumulation of soybean glycinin and its assembly with the glutelins in rice

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Saline-soluble glycinins and insoluble glutelins are the major storage proteins in soybean (Glycine max) and rice (Oryza sativa), respectively. In spite of their differences in solubility properties, both proteins are members of the 11S globulin gene family based on their similarities in primary

Identification and variation of glutelin alpha polypeptides in the genus Oryza assessed by two-dimensional electrophoresis and step-by-step immunodetection.

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To obtain fundamental information for nutritional improvement of rice (Oryza sativa) seed proteins, the alpha polypeptides of the major storage protein glutelin varied over the genus Oryza were qualitatively and quantitatively characterized with unique methods. The polypeptides were maximally

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