Base de dados : MEDLINE
Pesquisa : B01.650.940.800.575.912.250.157.175 [Categoria DeCS]
Referências encontradas : 160 [refinar]
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  1 / 160 MEDLINE  
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[PMID]:28745425
[Au] Autor:Filipov Y; Domanskyi S; Wood ML; Gamella M; Privman V; Katz E
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, 13699, USA.
[Ti] Título:Experimental Realization of a High-Quality Biochemical XOR Gate.
[So] Source:Chemphyschem;18(20):2908-2915, 2017 Oct 19.
[Is] ISSN:1439-7641
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We report an experimental realization of a biochemical XOR gate function that avoids many of the pitfalls of earlier realizations based on biocatalytic cascades. Inputs-represented by pairs of chemicals-cross-react to largely cancel out when both are nearly equal. The cross-reaction can be designed to also optimize gate functioning for noise handling. When not equal, the residual inputs are further processed to result in the output of the XOR type, by biocatalytic steps that allow for further gate-function optimization. The quality of the realized XOR gate is theoretically analyzed.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Oxirredutases do Álcool/metabolismo
Biocatálise
Glucose Oxidase/metabolismo
Hexoquinase/metabolismo
NAD/metabolismo
Peroxidase/metabolismo
[Mh] Termos MeSH secundário: Armoracia/enzimologia
Aspergillus niger/enzimologia
Modelos Moleculares
Pichia/enzimologia
Saccharomyces cerevisiae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0U46U6E8UK (NAD); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.3.13 (alcohol oxidase); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.7 (Peroxidase); EC 2.7.1.1 (Hexokinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1002/cphc.201700705


  2 / 160 MEDLINE  
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[PMID]:29327227
[Au] Autor:Khan A; Shrestha A; Bhuyan K; Maiti IB; Dey N
[Ad] Endereço:Department of Gene Function and Regulation, Department of Biotechnology, Government of India, Institute of Life Sciences, Chandrasekharpur, Bhubaneswar, Odisha, India.
[Ti] Título:Structural characterization of a novel full-length transcript promoter from Horseradish Latent Virus (HRLV) and its transcriptional regulation by multiple stress responsive transcription factors.
[So] Source:Plant Mol Biol;96(1-2):179-196, 2018 Jan.
[Is] ISSN:1573-5028
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: The promoter fragment described in this study can be employed for strong transgene expression under both biotic and abiotic stress conditions. Plant-infecting Caulimoviruses have evolved multiple regulatory mechanisms to address various environmental stimuli during the course of evolution. One such mechanism involves the retention of discrete stress responsive cis-elements which are required for their survival and host-specificity. Here we describe the characterization of a novel Caulimoviral promoter isolated from Horseradish Latent Virus (HRLV) and its regulation by multiple stress responsive Transcription factors (TFs) namely DREB1, AREB1 and TGA1a. The activity of full length transcript (Flt-) promoter from HRLV (- 677 to + 283) was investigated in both transient and transgenic assays where we identified H12 (- 427 to + 73) as the highest expressing fragment having ~ 2.5-fold stronger activity than the CaMV35S promoter. The H12 promoter was highly active and near-constitutive in the vegetative and reproductive parts of both Tobacco and Arabidopsis transgenic plants. Interestingly, H12 contains a distinct cluster of cis-elements like dehydration-responsive element (DRE-core; GCCGAC), an ABA-responsive element (ABRE; ACGTGTC) and as-1 element (TGACG) which are known to be induced by cold, drought and pathogen/SA respectively. The specific binding of DREB1, AREB1 and TGA1a to DRE, ABRE and as-1 elements respectively were confirmed by the gel-binding assays using H12 promoter-specific probes. Detailed mutational analysis of the H12 promoter suggested that the presence of DRE-core and as-1 element was indispensable for its activity which was further confirmed by the transactivation assays. Our studies imply that H12 could be a valuable genetic tool for regulated transgene expression under diverse environmental conditions.
[Mh] Termos MeSH primário: Armoracia/metabolismo
Armoracia/virologia
Caulimovirus/genética
Caulimovirus/metabolismo
Regiões Promotoras Genéticas/genética
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Arabidopsis/virologia
Armoracia/genética
Regulação da Expressão Gênica de Plantas
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/metabolismo
Plantas Geneticamente Modificadas/virologia
Tabaco/genética
Tabaco/metabolismo
Tabaco/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Transcription Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1007/s11103-017-0693-6


  3 / 160 MEDLINE  
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[PMID]:28764045
[Au] Autor:Pellicer JA; Gómez-López VM
[Ad] Endereço:Departamento de Ciencia y Tecnología de Alimentos, Universidad Católica de Murcia (UCAM), Campus de los Jerónimos 135, Guadalupe 30107, Murcia, Spain. Electronic address: japellicer@ucam.edu.
[Ti] Título:Pulsed light inactivation of horseradish peroxidase and associated structural changes.
[So] Source:Food Chem;237:632-637, 2017 Dec 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pulsed light (PL) is a non-thermal preservation method in which foods are subjected to one or several intense pulses of wide-spectrum light. Peroxidase (POD) is an enzyme that needs to be inactivated or inhibited because of its deleterious effects on the quality of fruits and vegetables. The feasibility of using PL to inactivate POD was tested and results explained based on measurements of UV-vis spectrum, far-UV circular dichroism and tryptophan fluorescence, and the phase-diagram method. PL reduced the activity of POD by more than 95% after applying 128Jcm . There was observed a decrease in the Reinheitzahl value and ellipticity and an increase in tryptophan fluorescence at incremental fluences, as well as linear phase diagrams. The study indicates that the inactivation of POD by PL is an all-or-none process related to loss of helical structure, weak unfolding and ejection of the prostetic group.
[Mh] Termos MeSH primário: Armoracia/enzimologia
Peroxidase do Rábano Silvestre/metabolismo
[Mh] Termos MeSH secundário: Dicroísmo Circular
Luz
Verduras
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.11.1.- (Horseradish Peroxidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


  4 / 160 MEDLINE  
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[PMID]:28490098
[Au] Autor:Kroener EM; Buettner A
[Ad] Endereço:Department of Chemistry and Pharmacy, Emil Fischer Center, Friedrich-Alexander-Universität Erlangen-Nürnberg, Henkestrasse 9, 91054 Erlangen, Germany. Electronic address: eva-maria.kroener@fau.de.
[Ti] Título:Unravelling important odorants in horseradish (Armoracia rusticana).
[So] Source:Food Chem;232:455-465, 2017 Oct 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Horseradish (Armoracia rusticana) is a plant well known for its roots' spicy aroma. The present study investigates the main aroma constituents of horseradish roots in general by analysing the aroma profiles of six different horseradish varieties, with one variety grown in two different soils. Odorants were characterised by means of gas chromatography-olfactometry and identified via their mass spectra, retention indices on two columns with different polarity, and their characteristic odour. A series of new aroma compounds from different substance groups were identified that have hitherto not been described in horseradish. Moreover, several of these constituents were successfully shown to exhibit high odour potency, alongside a high potential to influence the overall aroma of horseradish roots, like (3S,3aS,7aR)-wine lactone and 3-isopropyl-2-methoxypyrazine.
[Mh] Termos MeSH primário: Armoracia
Odorantes
[Mh] Termos MeSH secundário: Cromatografia Gasosa
Cromatografia Gasosa-Espectrometria de Massas
Olfatometria
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE


  5 / 160 MEDLINE  
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[PMID]:28490082
[Au] Autor:Dekic MS; Radulovic NS; Stojanovic NM; Randjelovic PJ; Stojanovic-Radic ZZ; Najman S; Stojanovic S
[Ad] Endereço:Department of Chemistry, Faculty of Science and Mathematics, University of Nis, Visegradska 33, 18000 Nis, Serbia; Department of Chemical and Technological Sciences, State University of Novi Pazar, Vuka Karadzica bb, 36300 Novi Pazar, Serbia.
[Ti] Título:Spasmolytic, antimicrobial and cytotoxic activities of 5-phenylpentyl isothiocyanate, a new glucosinolate autolysis product from horseradish (Armoracia rusticana P. Gaertn., B. Mey. & Scherb., Brassicaceae).
[So] Source:Food Chem;232:329-339, 2017 Oct 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Detailed analyses of horseradish autolysates led to the identification of a new natural product, 5-phenylpentyl isothiocyanate (PhPeITC). The structural assignment was corroborated by synthesis, and the identity unequivocally established by spectral means. The occurrence of PhPeITC is the first direct proof of the existence of a 5-phenylpentyl glucosinolate in the aerial parts of this species as one of the possible "mustard oil" precursors. To verify its possible contribution to the horseradish functional food status, horseradish above- and underground autolysates, together with five ω-phenylalkyl isothiocyanates were tested for their spasmolytic, cytotoxic and antimicrobial activities. Specifically, the cytotoxic effect on Caco-2, HeLa (cancer) and MDCK (non-cancer) cell lines was established. Additionally, the five tested ITCs exerted significant spasmolytic activity (on rat distal colon), with PhPeITC being almost 100 times more potent than papaverine. A non-selective antimicrobial activity of all ITCs was revealed in the case of 6 bacterial and 2 fungal strains.
[Mh] Termos MeSH primário: Armoracia/química
Glucosinolatos/química
Isotiocianatos/isolamento & purificação
[Mh] Termos MeSH secundário: Anti-Infecciosos/química
Anti-Infecciosos/farmacologia
Células CACO-2
Seres Humanos
Isotiocianatos/farmacologia
Parassimpatolíticos/química
Parassimpatolíticos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Glucosinolates); 0 (Isothiocyanates); 0 (Parasympatholytics)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE


  6 / 160 MEDLINE  
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[PMID]:28173696
[Au] Autor:Dahili LA; Nagy E; Feczkó T
[Ad] Endereço:Doctoral School of Molecular and Nanotechnologies, Research Institute of Chemical and Process Engineering, University of Pannonia, H-8200 Veszprém, Hungary.
[Ti] Título:2,4-Dichlorophenol Enzymatic Removal and Its Kinetic Study Using Horseradish Peroxidase Crosslinked to Nano Spray-Dried Poly(Lactic-Co-Glycolic Acid) Fine Particles.
[So] Source:J Microbiol Biotechnol;27(4):768-774, 2017 Apr 28.
[Is] ISSN:1738-8872
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:Horseradish peroxidase (HRP) catalyzes the oxidation of aromatic compounds by hydrogen peroxide via insoluble polymer formation, which can be precipitated from the wastewater. For HRP immobilization, poly(lactic-co-glycolic acid) (PLGA) fine carrier supports were produced by using the Nano Spray Dryer B-90. Immobilized HRP was used to remove the persistent 2,4-dichlorophenol from model wastewater. Both extracted (9-16 U/g) and purified HRP (11-25 U/g) retained their activity to a high extent after crosslinking to the PLGA particles. The immobilized enzyme activity was substantially higher in both the acidic and the alkaline pH regions compared with the free enzyme. Optimally, 98% of the 2,4-dichlorophenol could be eliminated using immobilized HRP due to catalytic removal and partly to adsorption on the carrier supports. Immobilized enzyme kinetics for 2,4-dichlorophenol elimination was studied for the first time, and it could be concluded that competitive product inhibition took place.
[Mh] Termos MeSH primário: Clorofenóis/metabolismo
Enzimas Imobilizadas/metabolismo
Peroxidase do Rábano Silvestre/metabolismo
Ácido Láctico/química
Nanopartículas/química
Ácido Poliglicólico/química
[Mh] Termos MeSH secundário: Adsorção
Armoracia/enzimologia
Catálise
Ensaios Enzimáticos
Estabilidade Enzimática
Peroxidase do Rábano Silvestre/química
Concentração de Íons de Hidrogênio
Cinética
Microscopia Eletrônica de Varredura
Nanopartículas/ultraestrutura
Extratos Vegetais/química
Temperatura Ambiente
Águas Residuais
Purificação da Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chlorophenols); 0 (Enzymes, Immobilized); 0 (Plant Extracts); 0 (Waste Water); 0 (polylactic acid-polyglycolic acid copolymer); 26009-03-0 (Polyglycolic Acid); 33X04XA5AT (Lactic Acid); EC 1.11.1.- (Horseradish Peroxidase); R669TG1950 (2,4-dichlorophenol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.4014/jmb.1606.06002


  7 / 160 MEDLINE  
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[PMID]:27313156
[Au] Autor:Gonda S; Kiss-Szikszai A; Szucs Z; Nguyen NM; Vasas G
[Ad] Endereço:Department of Botany, Division of Pharmacognosy, University of Debrecen, Egyetem tér 1, H-4010, Debrecen, Hungary.
[Ti] Título:Myrosinase Compatible Simultaneous Determination of Glucosinolates and Allyl Isothiocyanate by Capillary Electrophoresis Micellar Electrokinetic Chromatography (CE-MEKC).
[So] Source:Phytochem Anal;27(3-4):191-8, 2016 May.
[Is] ISSN:1099-1565
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: The functional food Cruciferous vegetables contain glucosinolates which are decomposed by the myrosinase enzyme upon tissue damage. The isothiocyanates are the most frequent decomposition products. Because of their various bioactivities, these compounds and the myrosinase is of high interest to many scientific fields. OBJECTIVE: Development of a capillary electrophoresis method capable of myrosinase-compatible, simultaneous quantification of glucosinolates and isothiocyanates. METHODS: Capillary electrochromatography parameters were optimised, followed by optimisation of a myrosinase-compatible derivatisation procedure for isothiocyanates. Vegetable extracts (Brussels sprouts, horseradish, radish and watercress) were tested for myrosinase activity, glucosinolate content and isothiocyanate conversion rate. Allyl isothiocyanate was quantified in some food products. RESULTS: The method allows quantification of sinigrin, gluonasturtiin and allyl isothiocyanate after myrosinase compatible derivatisation in-vial by mercaptoacetic acid. The chromatograhpic separation takes 2.5 min (short-end injection) or 15 min (long-end injection). For the tested vegetables, measured myrosinase activity was between 0.960-27.694 and 0.461-26.322 µmol/min/mg protein, glucosinolate content was between 0-2291.8 and 0-248.5 µg/g fresh weight for sinigrin and gluconastrutiin, respectively. The possible specificity of plants to different glucosinolates was also shown. Allyl isothiocyanate release rate was different in different vegetables (73.13 - 102.13%). The method could also be used for quantification of allyl isothiocyanate from food products. CONCLUSIONS: The presented capillary electrophoresis method requires a minimal amount of sample and contains only a few sample preparation steps, and can be used in several applications (glucosinolate determination, myrosinase activity measurement, isothiocyanate release estimation). Copyright © 2016 John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Cromatografia Capilar Eletrocinética Micelar/métodos
Eletroforese Capilar/métodos
Glucosinolatos/análise
Glicosídeo Hidrolases/análise
Isotiocianatos/análise
Extratos Vegetais/química
Verduras/química
[Mh] Termos MeSH secundário: Armoracia/química
Armoracia/enzimologia
Brassica/química
Brassica/enzimologia
Glucosinolatos/metabolismo
Glicosídeo Hidrolases/metabolismo
Isotiocianatos/metabolismo
Estrutura Molecular
Nasturtium/química
Nasturtium/enzimologia
Raphanus/química
Raphanus/enzimologia
Sensibilidade e Especificidade
Fatores de Tempo
Verduras/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucosinolates); 0 (Isothiocyanates); 0 (Plant Extracts); 50UM64RMBJ (sinigrin); BN34FX42G3 (allyl isothiocyanate); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.147 (thioglucosidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160618
[St] Status:MEDLINE
[do] DOI:10.1002/pca.2615


  8 / 160 MEDLINE  
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[PMID]:27272511
[Au] Autor:Bertóti R; Vasas G; Gonda S; Nguyen NM; Szoke É; Jakab Á; Pócsi I; Emri T
[Ad] Endereço:Department of Pharmacognosy, Semmelweis University, Budapest, Hungary.
[Ti] Título:Glutathione protects Candida albicans against horseradish volatile oil.
[So] Source:J Basic Microbiol;56(10):1071-1079, 2016 Oct.
[Is] ISSN:1521-4028
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Horseradish essential oil (HREO; a natural mixture of different isothiocyanates) had strong fungicide effect against Candida albicans both in volatile and liquid phase. In liquid phase this antifungal effect was more significant than those of its main components allyl, and 2-phenylethyl isothiocyanate. HREO, at sublethal concentration, induced oxidative stress which was characterized with elevated superoxide content and up-regulated specific glutathione reductase, glutathione peroxidase, catalase and superoxide dismutase activities. Induction of specific glutathione S-transferase activities as marker of glutathione (GSH) dependent detoxification was also observed. At higher concentration, HREO depleted the GSH pool, increased heavily the superoxide production and killed the cells rapidly. HREO and the GSH pool depleting agent, 1-chlore-2,4-dinitrobenzene showed strong synergism when they were applied together to kill C. albicans cells. Based on all these, we assume that GSH metabolism protects fungi against isothiocyanates.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Armoracia/metabolismo
Candida albicans/efeitos dos fármacos
Glutationa/metabolismo
Isotiocianatos/farmacologia
Óleos Voláteis/farmacologia
[Mh] Termos MeSH secundário: Catalase/metabolismo
Dinitroclorobenzeno/farmacologia
Sinergismo Farmacológico
Glutationa Peroxidase/metabolismo
Glutationa Redutase/metabolismo
Glutationa Transferase/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Superóxido Dismutase/metabolismo
Superóxidos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Isothiocyanates); 0 (Oils, Volatile); 11062-77-4 (Superoxides); 6U7TFK75KV (phenethyl isothiocyanate); BN34FX42G3 (allyl isothiocyanate); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); EC 1.8.1.7 (Glutathione Reductase); EC 2.5.1.18 (Glutathione Transferase); GAN16C9B8O (Glutathione); GE3IBT7BMN (Dinitrochlorobenzene)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170217
[Lr] Data última revisão:
170217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE
[do] DOI:10.1002/jobm.201600082


  9 / 160 MEDLINE  
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[PMID]:27081794
[Au] Autor:Wang L; Cheng M; Chu Y; Li X; Chen DDY; Huang X; Zhou Q
[Ad] Endereço:Jiangsu Collaborative Innovation Center of Biomedical Functional Materials, Jiangsu Key Laboratory of Biomedical Materials, School of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210046, PR China; State Key Laboratory of Food Science and Technology, School of Environment and C
[Ti] Título:Responses of plant calmodulin to endocytosis induced by rare earth elements.
[So] Source:Chemosphere;154:408-415, 2016 Jul.
[Is] ISSN:1879-1298
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The wide application of rare earth elements (REEs) have led to their diffusion and accumulation in the environment. The activation of endocytosis is the primary response of plant cells to REEs. Calmodulin (CaM), as an important substance in calcium (Ca) signaling systems, regulating almost all of the physiological activities in plants, such as cellular metabolism, cell growth and division. However, the response of CaM to endocytosis activated by REEs remains unknown. By using immunofluorescence labeling and a confocal laser scanning microscope, we found that trivalent lanthanum [La(III)], an REE ion, affected the expression of CaM in endocytosis. Using circular dichroism, X-ray photoelectron spectroscopy and computer simulations, we demonstrated that a low concentration of La(III) could interact with extracellular CaM by electrostatic attraction and was then bound to two Ca-binding sites of CaM, making the molecular structure more compact and orderly, whereas a high concentration of La(III) could be coordinated with cytoplasmic CaM or bound to other Ca-binding sites, making the molecular structure more loose and disorderly. Our results provide a reference for revealing the action mechanisms of REEs in plant cells.
[Mh] Termos MeSH primário: Arabidopsis/metabolismo
Armoracia/metabolismo
Calmodulina/metabolismo
Endocitose/fisiologia
Metais Terras Raras/farmacologia
Folhas de Planta/metabolismo
Fenômenos Fisiológicos Vegetais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Arabidopsis/efeitos dos fármacos
Arabidopsis/crescimento & desenvolvimento
Armoracia/efeitos dos fármacos
Armoracia/crescimento & desenvolvimento
Calmodulina/química
Dicroísmo Circular
Simulação por Computador
Endocitose/efeitos dos fármacos
Imunofluorescência
Microscopia Confocal
Modelos Moleculares
Espectroscopia Fotoeletrônica
Folhas de Planta/efeitos dos fármacos
Folhas de Planta/crescimento & desenvolvimento
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calmodulin); 0 (Metals, Rare Earth)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160416
[St] Status:MEDLINE


  10 / 160 MEDLINE  
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[PMID]:26747440
[Au] Autor:Sekuljica NZ; Prlainovic NZ; Jovanovic JR; Stefanovic AB; Djokic VR; Mijin DZ; Knezevic-Jugovic ZD
[Ad] Endereço:Faculty of Technology and Metallurgy, Innovation Center, University of Belgrade, Karnegijeva 4, 11000, Belgrade, Republic of Serbia.
[Ti] Título:Immobilization of horseradish peroxidase onto kaolin.
[So] Source:Bioprocess Biosyst Eng;39(3):461-72, 2016 Mar.
[Is] ISSN:1615-7605
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Kaolin showed as a very perspective carrier for the enzyme immobilization and it was used for the adsorption of horseradish peroxidase (HRP). The effects of the enzyme concentration and pH on the immobilization efficiency were studied in the reaction with pyrogallol and anthraquinone dye C.I. Acid Violet 109 (AV 109). In addition, Fourier transform infrared spectroscopy, scanning electron microscopy and analysis by Brunauer-Emmett-Teller were performed for kaolin, thermally activated kaolin and the immobilized enzyme. It has been shown that 0.1 IU of HRP-kaolin decolorized 87 % of dye solution, under the optimal conditions (pH 5.0, temperature 24 °C, dye concentration 40 mg/L and 0.2 mM of H2O2) within 40 min. The immobilized HRP decolorization follows the Ping Pong Bi-Bi mechanism with dead-end inhibition by the dye. The biocatalyst retained 35 ± 0.9 % of the initial activity after seven cycles of reuse in the decolorization reaction of AV 109 under optimal conditions in a batch reactor. The obtained kinetic parameters and reusability study confirmed improvement in performances of k-HRP compared to free, indicating that k-HRP has a great potential for environmental purposes.
[Mh] Termos MeSH primário: Armoracia/química
Enzimas Imobilizadas/química
Caulim/química
Proteínas de Plantas/química
[Mh] Termos MeSH secundário: Peroxidase do Rábano Silvestre/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Plant Proteins); 24H4NWX5CO (Kaolin); EC 1.11.1.- (Horseradish Peroxidase)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160110
[St] Status:MEDLINE
[do] DOI:10.1007/s00449-015-1529-x



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