globulin/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

Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy.

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The conformation of rice globulin (10%, w/v, in deuterated phosphate buffer, pD 7.4) under the influence of pH, chaotropic salts, several protein structure perturbants and heat treatments was studied by Fourier-transform infrared (FTIR) spectroscopy. Rice globulin exhibited seven major bands in the

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

Proteins and amino acids of some local varieties of rice seeds (Oryza Sativa L.).

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Proteins and amino acids in four local rice (Oryza Sativa L.) varieties were identified. Albumin and globulin were extracted from rice seeds, and the major promoters of these proteins were investigated by polyacrylamide gel electrophoresis to show their patterns. Amino acid composition of the rice

Nucleotide sequence of an abundant rice seed globulin: homology with the high molecular weight glutelins of wheat, rye and triticale.

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A cDNA clone corresponding to a 19 kD salt-soluble globulin of rice (Oryza sativa L.) was isolated by screening a lambda gt11 expression library of endosperm mRNA with antibodies raised against the purified rice seed alpha-globulin. The cDNA contained a single large open reading frame encoding a

Proteomic analysis of rice (Oryza sativa) seeds during germination.

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Although seed germination is a major subject in plant physiological research, there is still a long way to go to elucidate the mechanism of seed germination. Recently, functional genomic strategies have been applied to study the germination of plant seeds. Here, we conducted a proteomic analysis of

Expression and functional validation of heat-labile enterotoxin B (LTB) and cholera toxin B (CTB) subunits in transgenic rice (Oryza sativa).

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We expressed the heat-labile enterotoxin B (LTB) subunit from enterotoxigenic Escherichia coli and the cholera toxin B (CTB) subunit from Vibrio cholerae under the control of the rice (Oryza sativa) globulin (Glb) promoter. Binding of recombinant LTB and CTB proteins was confirmed based on

Genetic Basis of Variation in Rice Seed Storage Protein (Albumin, Globulin, Prolamin, and Glutelin) Content Revealed by Genome-Wide Association Analysis.

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Rice seed storage protein (SSP) is an important source of nutrition and energy. Understanding the genetic basis of SSP content and mining favorable alleles that control it will be helpful for breeding new improved cultivars. An association analysis for SSP content was performed to identify

Changes in protein expression profiles between a low phytic acid rice ( Oryza sativa L. Ssp. japonica) line and its parental line: a proteomic and bioinformatic approach.

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The seed proteome of a low phytic acid (lpa) rice line (Os-lpa-XS110-1), developed as a novel food source, was compared to that of its parental line, Xiushui 110 (XS-110). Analysis by surfaced enhanced laser desorption ionization-time-of-flight mass spectrometry (SELDI-TOF MS) and two-dimensional

Influence of high temperature during grain filling on the accumulation of storage proteins and grain quality in rice (Oryza sativa L.).

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The present study was performed to understand the effects of high temperature (HT) during filling on the expression of storage proteins and the quality of rice grains. HT (35/30 °C day/night) reduced the weight, amylose content, and flour gel consistency of grains. It increased the accumulation of

Distinct roles of protein disulfide isomerase and P5 sulfhydryl oxidoreductases in multiple pathways for oxidation of structurally diverse storage proteins in rice.

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In the rice (Oryza sativa) endosperm, storage proteins are synthesized on the rough endoplasmic reticulum (ER), in which prolamins are sorted to protein bodies (PBs) called type-I PB (PB-I). Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a

The small GTPase Rab5a is essential for intracellular transport of proglutelin from the Golgi apparatus to the protein storage vacuole and endosomal membrane organization in developing rice endosperm.

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Rice (Oryza sativa) glutelins are synthesized on the endoplasmic reticulum as larger precursors, which are then transported via the Golgi to the protein storage vacuole (PSV), where they are processed into acidic and basic subunits. Three independent glutelin precursor mutant4 (glup4) rice lines,

Biosynthesis of storage proteins in developing rice seeds.

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Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of the starchy endosperm protein of rice (Oryza sativa L. Japonica cv Koshihikari) during seed development confirmed that storage protein begins to accumulate about 5 days after flowering. Two polypeptide groups, 22 to 23 and 37 to

Proteomic analysis of cytoskeleton-associated RNA binding proteins in developing rice seed.

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In eukaryotes, RNA binding proteins (RBPs) play an integral role not only in RNA processing within the nucleus, but also in the cytoplasmic events of RNA transport, localization, translation, storage and degradation. While many studies have been done, relatively little is known about RBPs in plants.

Generation of transgenic rice lines with reduced contents of multiple potential allergens using a null mutant in combination with an RNA silencing method.

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Rice seed proteins are known to be a causative antigen in some patients with food allergy, especially cereal allergy, with clinical symptoms such as eczema and dermatitis. The α-amylase/trypsin inhibitors (14-16 kDa), α-globulin (26 kDa) and β-glyoxalase I (33 kDa) are regarded as major potential

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