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'Peroxidase' in keywords
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1Author    Gerold Baier, Peter Urban, Klaus WegmannRequires cookie*
 Title     
 Abstract    N e w M o d e l S y s te m fo r th e S tu d y o f C o m p le x D y n a m ic a l E n z y m e R e a c tio n s . I. A N o n lin e a r E n z y m e R e a c tio n in a C h e m ic a l G r a d ie n t An experimental system for the study of biochemical reaction dynamics is introduced and de­ scribed. A one-enzyme reaction is extended by an artificial feedback loop in an electrochemical device. Cyclic voltammetry is used to show that the reaction rate depends nonlinearly on the amount of cosubstrate offered. For some sets of fixed parameter values a damped oscillatory approach of the steady state was observed. The usefulness of the systems theoretical concepts is discussed. 
  Reference    Z. Naturforsch. 43a, 987—994 (1988); Received August 22 1988 
  Published    1988 
  Keywords    Reaction-diffusion Systems, Peroxidase, Feedback, Nonlinearity, Damped Oscillations 
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 TEI-XML for    default:Reihe_A/43/ZNA-1988-43a-0987.pdf 
 Identifier    ZNA-1988-43a-0987 
 Volume    43 
2Author    Jochen Berlin, Wolfgang BarzRequires cookie*
 Title    Oxidative Decarboxylation of /?^m-Hydroxybenzoic Acids by Peroxidases under in vivo and in vitro Conditions  
 Abstract    Oxidative decarboxylation of p-hydroxybenzoic acids in plant cell suspension cultures is catalyzed by peroxidases. This reaction has been characterized in vivo and in vitro. Decarboxylation of sub­ stituted benzoic acids yields monomeric, dimeric and oligomeric benzoquinones. All peroxidases ob­ tained from soybean (Glycine max) cell suspension cultures by gel electrophoresis are equally capable to decarboxylate p-hydroxybenzoic acids as indicated by their rather low differences in specific activity for various benzoic acids. 
  Reference    (Z. Naturforsch. 30c, 650—658 [1975]; received May 2911975) 
  Published    1975 
  Keywords    Decarboxylation, p-Hydroxybenzoic Acids, Peroxidases, Plant Cell Suspension Cultures 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0650.pdf 
 Identifier    ZNC-1975-30c-0650 
 Volume    30 
3Author    Martin Patzlaff, W. Olfgang BarzRequires cookie*
 Title    Peroxidatic Degradation of Flavanones  
 Abstract    Peroxidases were shown to be responsible for the degradation of flavanones as occuring after application of these substrates to plant cell suspension cultures. — Com parative studies with various flavanones and horseradish peroxidase showed th at only 4'-hydroxyflavanones will be catabolized peroxidatically. — Intensive analyses of naringenin (5,7,4'-trihydroxyflavanone) de­ gradation by horseradish peroxidase revealed that very complex reactions with m any catabolites are involved. Main degradative pathways comprise a) hydroxilation in the 3'-position, b) elim ina­ tion of ring B leading to chromones, c) cleavage reactions of the heterocylic ring resulting in phenolic catabolites from ring A and most im portant d) oxidative destruction of ring A leading to Cg — Cg-, Cs —C2-and C6—Cj-units from ring B. — The data are com pared with the results of feeding experiments and are discussed with regard to th eir physiological significance. 
  Reference    Z. Naturforsch. 33c, 675 (1978); received July 3 1978 
  Published    1978 
  Keywords    Flavanones, Catabolites, Peroxidases, D egradation, Substitution Pattern 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0675.pdf 
 Identifier    ZNC-1978-33c-0675 
 Volume    33 
4Author    Regina Volpert, ErichF. ElstnerRequires cookie*
 Title    Biochemical Activities of Propolis Extracts I. Standardization and Antioxidative Properties of Ethanolic and Aqueous Derivatives  
 Abstract    Ethanolic extracts of Propolis are used as antiinflammatory and wound healing drugs since ancient times. In order to facilitate a comparison of different extracts, the standardization on the basis of quantitative determination of prominent components of these extracts has been substituted for simple biochemical "activity" tests. One of these activity tests bases on the in­ hibition of peroxidase-catalyzed oxidation of indole acetic acid indicating the presence of a defined mixture of monophenolic and diphenolic compounds. Other tests (diaphorase-cata-lyzed reductions and xanthine oxidase-catalyzed oxidations) demonstrate significant radical scavenging properties. Water-soluble extracts of propolis exhibit higher antioxidative and inhibitory activities as compared to the ethanolic extract. 
  Reference    Z. Naturforsch. 48c, 851—857 (1993); received June 21/August 161993 
  Published    1993 
  Keywords    Propolis, Peroxidase, Xanthine Oxidase, Diaphorase, Indole Acetic Acid Oxidation 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0851.pdf 
 Identifier    ZNC-1993-48c-0851 
 Volume    48 
5Author    A. Kio Kobayashi, Yutaka Koguchi, Hiroshi Kanzaki, Shin-Ichiro Kajiyama, Kazuyoshi KawazuRequires cookie*
 Title    A New Type of Antimicrobial Phenolics Produced by Plant Peroxidase and Its Possible Role in the Chemical Defense Systems against Plant Pathogens  
 Abstract    Syringaldehyde readily reacted in the horse-radish peroxidase (H R P O D) system. The ethyl acetate extract of the reaction mixture showed a marked antimicrobial activity against bac­ teria and fungi. A fter repeated column chromatography three potential antimicrobial com ­ pounds were obtained from the extract. The structural elucidation of active compounds was achieved by a combination of spectroscopic techniques and chemical modification. 
  Reference    Z. Naturforsch. 49c, 411 (1994); received January 1/April 25 1994 
  Published    1994 
  Keywords    Peroxidase, Syringaldehyde, Phenolics, Antimicrobial Compounds, Chemical D efense System 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0411.pdf 
 Identifier    ZNC-1994-49c-0411 
 Volume    49 
6Author    Wolfgang Barz, Rita Schlepphorst, Peter Wilhelm, Westfalen, Karl Kratzl, Erich TenglerRequires cookie*
 Title    Metabolism of Benzoic Acids and Phenols in Cell Suspension Cultures of Soybean and Mung Bean  
 Abstract    Uptake of benzoic and salicylic acid by soybean cell suspension cultures is diffusion-mediated and exclusively leads to glucose-esters. — Veratric acid is para-demethylated to vanillic acid which is conjugated to a monoglucoside. — Nitrobenzoic acids are scarcely taken up by cell cultures with glucose-esters as sole products. — Ring-labelled derivatives of vanillylalcohol and creosol are mainly polymerized to insoluble structures, ring cleavage reactions could not be observed. 
  Reference    Z. Naturforsch. 33c, 363 (1978); received April 12 1978 
  Published    1978 
  Keywords    Benzoic Acids, Phenols, Ring Fission, Peroxidases, Polymerisation, Plant Cell Suspension Cultures 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0363.pdf 
 Identifier    ZNC-1978-33c-0363 
 Volume    33 
7Author    Johannes Kösler, Monika Ohm, Wolfgang BarzRequires cookie*
 Title    Metabolism of Anthranilic Acid in Plant Cell Suspension Cultures  
 Abstract    Cell suspension cultures of some 12 plants were investigated for anthranilic acid metabolism. Rapid uptake of substrate is accompanied by partial excretion of anthranilic acid-N-glucoside and followed by predominant conversion into tryptophan. Ring cleavage reactions of anthranilate could not be observed but peroxidatic polymerisation occurred to a high percentage. Anthranilic acid-N-glucoside is not permanently stored by the cell cultures. 
  Reference    Z. Naturforsch. 33c, 368 (1978); received April 19 1978 
  Published    1978 
  Keywords    Anthranilic Acid, Plant Cell Suspension Cultures, Tryptophan, Glucoside, Degradation, Peroxidases 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0368.pdf 
 Identifier    ZNC-1978-33c-0368 
 Volume    33 
8Author    Ralf Perrey, Marie-Theres Hauser, MichaelW. InkRequires cookie*
 Title    Cellular and Subcellular Localization of Peroxidase Isoenzymes in Plants and Cell Suspension Cultures from Lupinus polyphyllus  
 Abstract    , leaf protoplasts and cell suspension cultures of Lupinus polyphyllus and isolated vacuoles were studied for cellular and subcellular localization of peroxidase isoenzymes. Isoelectric focusing revealed 16 peroxidase isoenzymes. The basic peroxidase isoenzymes are predominantly localized in the vacuole and, to a minor degree, unbound in the intercellular space. The acidic isoenzymes are cell wall-bound in plants and not detectable in suspension-cultured cells. Large amounts (up to 11.0 U/ml) of a single basic isoenzyme are detectable in the spent medium of cell suspension cultures. 
  Reference    Z. Naturforsch. 44c, 931—936 (1989); received August 4 1989 
  Published    1989 
  Keywords    Lupinus, Peroxidase, Localization, Isoelectric Focusing (Peroxidase), Cell Culture Leaves, stems, roots 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0931.pdf 
 Identifier    ZNC-1989-44c-0931 
 Volume    44