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Archives of biochemistry and biophysics, ISSN 0003-9861, 05/2015, Volume 574, pp. 108 - 119
Journal Article
Biochimie, ISSN 0300-9084, 03/2012, Volume 94, Issue 3, pp. 673 - 683
Extracellular catalase–peroxidase | Oxidative stress | Phytopathogen | Reduction potential | Peroxidases–catalase superfamily | Resonance Raman spectroscopy | Extracellular catalase-peroxidase | Peroxidases-catalase superfamily | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Fungal Proteins - chemistry | Magnaporthe - enzymology | Oxidative Stress | Phylogeny | Catalase - classification | Peroxidases - classification | Catalase - metabolism | Peroxidases - chemistry | Magnaporthe - metabolism | Peroxidases - metabolism | Spectrum Analysis, Raman | Catalase - chemistry | Fungal Proteins - metabolism | Electrochemical reactions | Lignin | Hydrogen | Genes | Liquid chromatography | Cyanides | Raman spectroscopy | Cytochrome c | Histidine | Codon | Ionization | Hydroxylapatite | Heme | Electrochemistry | Peroxidase | Chemical properties | Mass spectrometry | Phenylalanine | Resveratrol | Cyanide | Spectroscopy | Data processing | Mass spectroscopy | pH effects | Host-pathogen interactions | rice blast | Catalase | Phytopathogenic fungi | Adducts | Structure-function relationships | Index Medicus | MnP, manganese peroxidase | HGT, horizontal gene transfer | 6c, six-coordinated | ESI, electrospray ionization | MagKatG2, catalase–peroxidase from Magnaporthe grisea | IPTG, isopropyl-β-thiogalactopyranoside | QS, quantum mixed-spin | CcP, cytochrome c peroxidase | HS, high-spin | HRP, horseradish peroxidase | LC, liquid chromatography | MCD, monochlorodimedone | KatG1, intracellular eukaryotic catalase–peroxidase | 5c, five-coordinated | BP1, barley peroxidase type 1 | KatG, catalase–peroxidase | Research Paper | E°′, reduction potential, referred to the standard hydrogen electrode, measured at pH 7.0 | RT-PCR, reverse-transcription PCR | SBP, soybean peroxidase | SHE, standard hydrogen electrode | MOPS, 4-morpholinepropane sulfonic acid | CAI, codon adaptation index | CAPS, 3-(cyclohexylamino)propane-1-sulfonic acid | l-DOPA, 3,4-dihydroxy-l-phenylalanine | APx, ascorbate peroxidase | ARP, Arthromyces ramosus peroxidase | ECD, electronic CD | CT, charge transfer | RR, resonance Raman | OTTLE, optically transparent thin-layer electrochemistry | MCAC, metal chelate affinity chromatography | LS, low-spin | CCD, charge-coupled device | NJ, neighbor-joining method | CIP, Coprinus cinereus peroxidase | LiP, lignin peroxidase | HA, hydroxyapatite | KatG2, extracellular eukaryotic catalase–peroxidase
Journal Article
Journal of the science of food and agriculture, ISSN 0022-5142, 08/2017, Volume 97, Issue 10, pp. 3249 - 3260
germination | phenol | temperature stability | peroxidase | green gram | p‐chlorophenol | p-chlorophenol | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Food Science & Technology | Agriculture, Multidisciplinary | Agriculture | Science & Technology | Enzymes, Immobilized - metabolism | Vigna - chemistry | Plant Roots - genetics | Enzymes, Immobilized - isolation & purification | Peroxidase - chemistry | Phenol - metabolism | Plant Proteins - chemistry | Vigna - enzymology | Plant Proteins - metabolism | Chlorophenols - metabolism | Plant Roots - growth & development | Plant Proteins - isolation & purification | Enzymes, Immobilized - chemistry | Plant Roots - metabolism | Enzyme Stability | Vigna - growth & development | Vigna - genetics | Peroxidase - isolation & purification | Plant Proteins - genetics | Water Pollutants, Chemical - metabolism | Enzymes, Immobilized - genetics | Plant Roots - enzymology | Peroxidase - genetics | Kinetics | Hydrogen-Ion Concentration | Peroxidase - metabolism | Physiological aspects | Phenols | Cysteine | Peroxidase | Germination | p-Chlorophenol | Temperature | Hydrogen peroxide | Enzyme activity | Roots | Horseradish peroxidase | Optimization | Molecular weight | Enzymatic activity | Temperature effects | Electrophoresis | Extraction | Oxidation | Physiology | Copper | Dithiothreitol | Enzymes | Stability | Purification | Gel electrophoresis | Wastewater | Phenolic compounds | Substrates | o-Dianisidine | Chlorophenol | Sodium | Homogeneity | Index Medicus
Journal Article
Food chemistry, ISSN 0308-8146, 2009, Volume 115, Issue 4, pp. 1177 - 1186