peroxidase/tupakat

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"Chitin-specific" peroxidases in plants.

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The activity of various plant peroxidases and the ability of their individual isoforms to bind chitin was studied. Some increase in peroxidase activity was observed in crude extracts in the presence of chitin. Activated peroxidases of some species fell in the fraction not sorbed on chitin and those

Real-time quantification of methanol in plants using a hybrid alcohol oxidase-peroxidase biosensor.

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An amperometric biosensor immobilizing two enzymes and an electron mediator in an identical plane has been fabricated by the self-assembly technique for determination of methanol in crude plant samples. A self-assembled mixed monolayer of 4,4'-dithiodibutyric acid covalently attached two enzymes

Role of peroxidase in lignification of tobacco cells : I. Oxidation of nicotinamide adenine dinucleotide and formation of hydrogen peroxide by cell wall peroxidases.

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The two peroxidase isoenzyme groups (G(I) and G(III)) localized in the cell walls of tobacco (Nicotiana tabacum L.) tissues were compared with respect to their capacity for NADH-dependent H(2)O(2) formation. Peroxidases of the G(III) group are slightly more active than those of the G(I) group when

High-efficiency secretory production of peroxidase C1a using vesicular transport engineering in transgenic tobacco.

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Horseradish peroxidase isozyme C1a (HRP C1a) is widely used as a reporter enzyme in a variety of detection procedures such as enzyme-linked immunosorbent assay (ELISA) and western blotting. We previously isolated the gene encoding HRP C1a and showed that HRP C1a is at first translated as a

Tomato phospholipid hydroperoxide glutathione peroxidase inhibits cell death induced by Bax and oxidative stresses in yeast and plants.

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Using a conditional life or death screen in yeast, we have isolated a tomato (Lycopersicon esculentum) gene encoding a phospholipid hydroperoxide glutathione peroxidase (LePHGPx). The protein displayed reduced glutathione-dependent phospholipid hydroperoxide peroxidase activity, but differs from

[Cell-wall and peroxidase-isoenzyme synthesis in isolated protoplasts of Nicotiana tabacum L].

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Mesophyll-protoplasts of tobacco show increasing peroxidase-activity immediately after isolation. This is due to an enhancement of activity of the constitutive isoenzymes of GIII (=slow migrating cathodic group) and to a new formation of GII-isoenzymes (=slow migrating anodic group). (GII is not

Peroxidase-Induced Wilting in Transgenic Tobacco Plants.

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Peroxidases are a family of isoenzymes found in all higher plants. However, little is known concerning their role in growth, development, or response to stress. Plant peroxidases are heme-containing monomeric glycoproteins that utilize either H2O2 or O2 to oxidize a wide variety of molecules. To

De-novo synthesis and release of peroxidases in cell suspension cultures of Nicotiana tabacum L.

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De-novo synthesis of acid and basic peroxidases has been studied in cell suspension cultures of tobacco by incorporation of (3)H- and (14)C-amino acids. Incorporation rates were found to be high for acid peroxidases and low for basic peroxidases. Synthesis of all peroxidases was inhibited by

Superoxide dismutase and peroxidase are coordinately regulated in differentiated and transformed tissues of Nicotiana tabacum.

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We used a series of normal and Agrobacterium-transformed, bacteria-free tobacco tissue cultures which differ in their levels of histodifferentiation to test the relationship of superoxide dismutase, peroxidase, and catalase to oncogenic transformation and differentiation. When compared with normal

Examination of the biological effects of high anionic peroxidase production in tobacco plants grown under field conditions. I. Insect pest damage.

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At least 25 wild type and high peroxidase tobacco Nicotiana tabacum L. plants were examined semiweekly over several weeks for pest insect distribution and damage in a 2 year field study. Incidence and/or severity of naturally occurring caterpillar damage (dingy cutworm (Feltia ducens Walker), black

Overproduction of Ascorbate Peroxidase in the Tobacco Chloroplast Does Not Provide Protection against Ozone.

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Transgenic tobacco (Nicotiana tabacum cv Bel W3) plants were used to test the hypothesis that protection from O3 injury could be conferred by overproduction of ascorbate peroxidase (APX) in the chloroplast. The 10-fold increase in soluble APX activity in the chloroplast was expected to alleviate an

Expression of the tobacco anionic peroxidase gene is tissue-specific and developmentally regulated.

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Transcriptionally regulated expression of tobacco anionic peroxidase was investigated with regard to tissue specificity and developmental regulation. Two tobacco species, Nicotiana sylvestris and Nicotiana tabacum cv. Xanthi, were stably transformed with a gene chimera composed of 3 kb of the

[Regulation of peroxidase patterns during shoot differentiation in callus cultures of Nicotiana tabacum L].

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Peroxidase activity and isoenzyme pattern were studied during dedifferentiation of tobacco stem-sections leading to callus formation and during redifferentiation of tobacco callus leading to formation of shoots. These processes are both accompanied by an increase in total peroxidase activity and by

Vesicular transport route of horseradish C1a peroxidase is regulated by N- and C-terminal propeptides in tobacco cells.

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Peroxidases (PRX, EC 1.11.1.7) are widely distributed across microorganisms, plants, and animals; and, in plants, they have been implicated in a variety of secondary metabolic reactions. In particular, horseradish (Armoracia rusticana) root represents the main source of commercial PRX production.

Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: Molecular analysis and tissue-specific expression.

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Plant peroxidases play a major role in lignin formation and wound healing and are believed to be involved in auxin catabolism and defense to pathogen attack. The function of the anionic peroxidase isozymes is best understood in tobacco. These isozymes catalyze the formation of the lignin polymer and

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