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peroxidase/sója
Odkaz je uložen do schránky
Strana 1 z 154 Výsledek
Purification of soybean peroxidase (Glycine max) by metal affinity partitioning in aqueous two-phase systems.
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Přihlášení Registrace
Combining two concepts in downstream processing, this work investigates the partitioning of a crude soybean peroxidase (Glycine max) in an aqueous two-phase system by metal affinity. A liquid-liquid extraction process using metal ligands was developed in two steps with the aim of purifying the
Safety evaluation of the food enzyme peroxidase obtained from soybean ( Glycine max) hulls
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The food enzyme considered in this opinion is a peroxidase (hydrogen-peroxide oxidoreductase; EC 1.11.1.7) obtained from hulls of soybeans (Glycine max) by the company Kerry Ingredients & Flavours. The compositional data provided were considered sufficient. The manufacturing process did
Purification and Developmental Analysis of the Major Anionic Peroxidase from the Seed Coat of Glycine max.
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We show that the majority of peroxidase activity in soybean (Glycine max var Williams 82) seeds is localized to the seed coat. A single isozyme is responsible for this activity and has been purified to electrophoretic homogeneity by successive chromatography on DEAE Sepharose Fast Flow, concanavalin
The unlabelled-peroxidase antiperoxidase method used for the localization of leghaemoglobin in Glycine max nodules [proceedings].
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Laser capture microdissection (LCM) and comparative microarray expression analysis of syncytial cells isolated from incompatible and compatible soybean (Glycine max) roots infected by the soybean cyst nematode (Heterodera glycines).
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Syncytial cells in soybean (Glycine max cultivar [cv.] Peking) roots infected by incompatible and compatible populations of soybean cyst nematode (SCN [Heterodera glycines]) were collected using laser capture microdissection (LCM). Gene transcript abundance was assayed using Affymetrix soybean
Purification and characterization of novel cationic peroxidases from Asparagus acutifolius L. with biotechnological applications.
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Four novel basic peroxidases, named AaP-1, AaP-2, AaP-3, and AaP-4, were purified from Asparagus acutifolius L. seeds by cation-exchange and gel filtration chromatographies. The four proteins showed a similar electrophoretic mobility of 46 kDa while, by MALDI-TOF MS, different Mr values of 42758.3,
Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide.
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Anionic soybean peroxidase Glycine max (SbP) is shown to efficiently catalyze luminol oxidation by hydrogen peroxide. Contrary to horseradish peroxidase, the presence of p-iodophenol in the reaction medium affects slightly the efficiency of SbP catalysis. A maximal intensity of chemiluminescence,
Endophytic Paecilomyces formosus LHL10 Augments Glycine max L. Adaptation to Ni-Contamination through Affecting Endogenous Phytohormones and Oxidative Stress.
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This study investigated the Ni-removal efficiency of phytohormone-producing endophytic fungi Penicillium janthinellum, Paecilomyces formosus, Exophiala sp., and Preussia sp. Among four different endophytes, P. formosus LHL10 was able to tolerate up to 1 mM Ni in contaminated media as compared to
Effectiveness of phenoxyl radicals generated by peroxidase/H2O2-catalyzed oxidation of caffeate, ferulate, and p-coumarate in cooxidation of ascorbate and NADH.
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The rate of ascorbate and nicotinamide adenine dinucleotide plus hydrogen (NADH) cooxidation (i.e., their nonenzymic oxidation by peroxidase/H2O2-generated phenoxyl radicals of three hydroxycinnamates: caffeate, ferulate and p-coumarate) was studied in vitro. The reactions initiated by different
Transganglionic transport of the lectin soybean agglutinin (Glycine max) following injection into the sciatic nerve of the adult rat.
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The lectin soybean agglutinin (SBA) from Glycine max binds to small-sized dorsal root ganglion cells and their central terminals in the superficial dorsal horn of the spinal cord. Here we investigated the ability of SBA and SBA conjugated to horseradish peroxidase (SBA-HRP) to trace thin calibre
Rapid Accumulation of Anionic Peroxidases and Phenolic Polymers in Soybean Cotyledon Tissues following Treatment with Phytophthora megasperma f. sp. Glycinea Wall Glucan.
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Phytophthora megasperma Drechs. f. sp. glycinea Kuan & Erwin (PMG) cell wall glucan has been extensively characterized as an elicitor of the pterocarpan phytoalexins, the glyceollins in soybean (Glycine max L.). Just recently, this glucan was shown to be a potent elicitor of conjugates of the
L-DOPA increases lignification associated with Glycine max root growth-inhibition.
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L-3,4-dihydroxyphenylalanine (L: -DOPA), an allelochemical exuded from the roots of velvet bean [Mucuna pruriens (L.) DC. var. utilis], presents a highly inhibitory action to plant growth. The effects of L-DOPA on phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) and peroxidase (POD, EC 1.11.1.7)
Lectin receptors as markers of lymphoid cells. I. Demonstration in tissue section by peroxidase technique.
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The distribution of lectin binding receptors in human lymphoid tissue (lymph node and tonsil) was studied in an effort to identify lectins with potential application as cell markers. Using a simple peroxidase technique applicable to formalin-fixed, paraffin-embedded tissue, the binding properties of
Demonstration of sugar residues in the ultimobranchial tubule and thyroid C-cells of the rat using peroxidase labelled lectins.
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The distribution of various sugars, that contribute to the composition of the carbohydrate components of the glycoprotein in the ultimobranchial tubule and the thyroid C-cells has been studied, using eight peroxidase-labelled lectins (Dolichos biblorus, Glycine max, Bauhinia purpurea, Helix pomatia,
Histochemical characterization of glycoproteins present in jejunal and colonic goblet cells of pigs on different diets. A biopsy study using chemical methods and peroxidase-labelled lectins.
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We examined the glycoprotein composition of intestinal goblet cells in jejunal and colonic biopsies obtained from pigs on different diets. Paraffin sections were stained both chemically and with the following horseradish-peroxidase conjugated lectins: Canavalia ensiformis (Con-A), Limulus polyphemus
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