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peroxidase/oryza sativa
Krækjan er vistuð á klemmuspjaldið
Bls 1 frá 243 niðurstöður
Molecular cloning and characterization of two complementary DNAs encoding putative peroxidases from rice (Oryza sativa L.) shoots.
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PCR with oligonucleotide primers that corresponded to two highly homologous regions, in terms of amino acid sequence, of plant peroxidases was used to amplify a specific DNA fragment from a mixture of rice (Oryza sativa L.) cDNAs. We then screened a cDNA library prepared from mRNAs of rice shoots
Increased Activity of a Cationic Peroxidase Associated with an Incompatible Interaction Between Xanthomonas oryzae pv oryzae and Rice (Oryza sativa).
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Rice (Oryza sativa L.) cultivar Cas 209 carries the gene Xa-10 for resistance to race 2 of Xanthomonas oryzae pv oryzae, the bacterial blight pathogen. When seedling leaves of Cas 209 plants were infiltrated with bacterial cell suspensions of strain PXO86(Rif) (race 2, incompatible), total
Characterization of a new member of the glutathione peroxidase gene family in Oryza sativa.
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A cDNA encoding an Oryza sativa glutathione peroxidase, OsGPX1, was isolated and characterized. OsGPX1 encodes a protein of 168 amino acids with a predicted molecular mass of approximately 18.5 kDa. The protein has 92% identity to a GPX of Zea mays, but only 65% identity to rice PHGPX. The deduced
Fractionation and characterization of two forms of peroxidase from Oryza sativa.
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Peroxidase (E.C. 1.11.1.7., hydrogen donor oxidoreductase) is widely distributed and has been isolated from many higher plants (1). The wide distribution of the enzyme suggests that it could be of great biological importance. However the role that it plays in metabolism is not clear due to the large
Purification and physicochemical characterization of a recombinant phospholipid hydroperoxide glutathione peroxidase from Oryza sativa.
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Phospholipid hydroperoxide glutathione peroxidase (PHGPx) is an unique antioxidant enzyme that directly reduces lipid hydroperoxides in biomembranes. In the present work, the entire encoding region for Oryza sativa PHGPx was expressed in Escherichia coli M15, and the purified fusion protein showed a
NaCl-induced expression of ASCORBATE PEROXIDASE 8 in roots of rice (Oryza sativa L.) seedlings is not associated with osmotic component.
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Ascorbate peroxidase (APx; EC 1.11.1.11) plays an important role in scavenging the toxic effects of H(2)O(2) in higher plants. Eight types of APx have been described for Oryza sativa: two cytosolic (OsAPx1 and OsAPx2), two putative peroxisomal (OsAPx3 and OsAPx4), and four chloroplastic isoforms
Study of growth factors, alpha-amylase and peroxidase activity in various cultivars of rice (Oryza sativa L.) under vanillic acid stress.
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The effects of Vanillic Acid (VA) on germination, seedling and adult plant of rice (Oryza sativa L.) were investigated. Four cultivars, traditional (Taroom mahalli and Taroom deilamani) and improved (Shafagh and Onda) were studied. For germination, seeds were sterilized and then placed on Petri dish
Expression of ASCORBATE PEROXIDASE 8 in roots of rice (Oryza sativa L.) seedlings in response to NaCl.
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Reactive oxygen species are thought to play an important role in NaCl stress. Therefore, the expression patterns of the gene family encoding the H(2)O(2)-scavenging enzyme ascorbate peroxidase (APx; EC1.11.1.11) were analysed in roots of etiolated rice (Oryza sativa L.) seedlings in response to NaCl
Effects of microcystins on the growth and the activity of superoxide dismutase and peroxidase of rape (Brassica napus L.) and rice (Oryza sativa L.).
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Microcystins are naturally occurring hepatotoxic cyclic heptapeptides produced by some toxic freshwater cyanobacterial species. In this study, crude extract of toxic cyanobacterial blooms from Dianchi Lake in southwestern China was used to determine the effects of microcystins on rape (Brassica
Effects of signaling molecules, protein phosphatase inhibitors and blast pathogen (Magnaporthe grisea) on the mRNA level of a rice (Oryza sativa L.) phospholipid hydroperoxide glutathione peroxidase (OsPHGPX) gene in seedling leaves.
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With a specific focus on rice self-defense response(s), the effects of global signaling molecules, jasmonic acid (JA), salicylic acid (SA), abscisic acid (ABA), and ethylene (using the ethylene generator, ethephon), and protein phosphatase (PP) inhibitors, cantharidin and endothall on expression of
Analysis of peroxidase activity of rice (Oryza sativa) recombinant hemoglobin 1: implications for in vivo function of hexacoordinate non-symbiotic hemoglobins in plants.
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In plants, it has been proposed that hexacoordinate (class 1) non-symbiotic Hbs (nsHb-1) function in vivo as peroxidases. However, little is known about peroxidase activity of nsHb-1. We evaluated the peroxidase activity of rice recombinant Hb1 (a nsHb-1) by using the guaiacol/H2O2 system at pH 6.0
Purification and characterization of two ascorbate peroxidases of rice (Oryza sativa L.) expressed in Escherichia coli.
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To clarify the diversity and function of isozymes of ascorbate peroxidase (APX) in plants, a method of producing large quantities of these proteins is needed. Here, we describe an Escherichia coli expression system for the rapid and economic expression of two rice APX genes, APXa and APXb (GeneBank
Molecular cloning and expression of a phospholipid hydroperoxide glutathione peroxidase homolog in Oryza sativa.
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A cDNA encoding putative phospholipid hydroperoxide glutathione peroxidase (PHGPX) was isolated from rice using rapid amplification of cDNA ends. This cDNA, designated ricPHGPX, includes an open reading frame encoding a protein of 169 amino acids which shares about 60% and 50% amino acid sequence
GSH-dependent peroxidase activity of the rice (Oryza sativa) glutaredoxin, a thioltransferase.
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Glutaredoxin (Grx) is a 12-kDa thioltransferase that reduces disulfide bonds of other proteins and maintains the redox potential of cells. In addition to its oxidoreductase activity, we report here that a rice Grx (OsGrx) can also function as a GSH-dependent peroxidase. Because of this antioxidant
Comparative analysis of ascorbate peroxidases (APXs) from selected plants with a special focus on Oryza sativa employing public databases.
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Reactive oxygen species (ROS) are produced by plants. Hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital
Heillasta gagnagrunnur lækningajurtanna sem studdur er af vísindum
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