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[PMID]:29248929
[Au] Autor:Amasdl S; Smaili W; Natiq A; Hassani A; Sbiti A; Agadr A; Sanlaville D; Sefiani A
[Ad] Endereço:Centre de Génomique Humaine, Faculté de Médecine et de Pharmacie, Université Mohammed V Souissi, Rabat, Morocco.
[Ti] Título:Familial X/Y Translocation Encompassing ARSE in Two Moroccan Siblings with Sensorineural Deafness.
[So] Source:Cytogenet Genome Res;153(2):66-72, 2017.
[Is] ISSN:1424-859X
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Unbalanced translocations involving X and Y chromosomes are rare and associated with a contiguous gene syndrome. The clinical phenotype is heterogeneous including mainly short stature, chondrodysplasia punctata, ichthyosis, hypogonadism, and intellectual disability. Here, we report 2 brothers with peculiar gestalt, short stature, and hearing loss, who harbor an X/Y translocation. Physical examination, brainstem acoustic potential evaluation, bone age, hormonal assessment, and X-ray investigations were performed. Because of their dysmorphic features, karyotyping, FISH, and aCGH were carried out. The probands had short stature, hypertelorism, midface hypoplasia, sensorineural hearing loss, normal intelligence as well as slight radial and ulnar bowing with brachytelephalangy. R-banding identified a derivative X chromosome with an abnormally expanded short arm. The mother was detected as a carrier of the same aberrant X chromosome. aCGH disclosed a 3.1-Mb distal deletion of chromosome region Xp22.33pter. This interval encompasses several genes, especially the short stature homeobox (SHOX) and arylsulfatase (ARSE) genes. The final karyotype of the probands was: 46,Y,der(X),t(X;Y)(p22;q12).ish der(X)(DXYS129-,DXYS153-)mat.arr[hg19] Xp22.33(61091_2689408)×1mat,Xp22.33(2701273_3258404)×0mat,Yq11.222q12 (21412851_59310245)×2. Herein, we describe a Moroccan family with a maternally inherited X/Y translocation and discuss the genotype-phenotype correlations according to the deleted genes.
[Mh] Termos MeSH primário: Anormalidades Múltiplas/genética
Arilsulfatases/genética
Cromossomos Humanos X/genética
Cromossomos Humanos Y/genética
Perda Auditiva Bilateral/genética
Perda Auditiva Neurossensorial/genética
Translocação Genética
[Mh] Termos MeSH secundário: Arilsulfatases/deficiência
Cromossomos Humanos X/ultraestrutura
Cromossomos Humanos Y/ultraestrutura
Consanguinidade
Feminino
Seres Humanos
Hipertelorismo/genética
Recém-Nascido
Cariotipagem
Masculino
Meia-Idade
Marrocos
Linhagem
Fenótipo
Rádio (Anatomia)/anormalidades
Escoliose/genética
Irmãos
Ulna/anormalidades
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.6.- (ARSE protein, human); EC 3.1.6.1 (Arylsulfatases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE
[do] DOI:10.1159/000485071


  2 / 1413 MEDLINE  
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[PMID]:28526525
[Au] Autor:Yang X; Feng Y; Chong H; Wang D; Hu X; Pu J; Zhan CG; Liao F
[Ad] Endereço:Unit for Analytical Probes and Protein Biotechnology, Key Laboratory of Medical Laboratory Diagnostics of the Education Ministry, College of Laboratory Medicine, Chongqing Medical University, Chongqing 400016, China.
[Ti] Título:High-throughput estimation of specific activities of enzyme/mutants in cell lysates through immunoturbidimetric assay of proteins.
[So] Source:Anal Biochem;534:91-98, 2017 Oct 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High-throughput estimation of specific activities of an enzyme and its mutants in a group (enzyme/mutants) in cell lysates via high-throughput assay of their activities and separate immunoturbidimetric assay (ITA) of their proteins was proposed. Pseudomonas aeruginosa arylsulfatase (PAAS) and Bacillus fastidious uricase (BFU) served as two models. ITA employed 0.75 mg of antisera against PAAS or BFU as the reference in 96-well microplates to measure the difference of extinction at 340 and 700 nm. According to the calibration curve, ITA quantified the reference from 0.40 to about 2.4 µg. The consistency among the abundance of enzyme/mutants through ITA of proteins in cell lysates prepared under the same conditions supported their consistent immunological reactivity to the antisera. Specific activities of PAAS/mutants or BFU/mutants in cell lysates through ITA of proteins showed excellent proportionality to those carefully determined after purification. Receiver-operating-characteristic (ROC) analysis of specific activities through ITA of proteins gave a higher area-under-curve than those for ROC analyses of other activity indices, which allowed the recognition of a PAAS/mutant of 50% higher activity after cell amplification in high-throughput mode. Therefore, ITA of enzyme/mutants as proteins is promising to estimate their specific activities in cell lysates in high-throughput mode for quantitative comparison.
[Mh] Termos MeSH primário: Arilsulfatases/análise
Ensaios de Triagem em Larga Escala
Técnicas Imunoenzimáticas
Urato Oxidase/análise
[Mh] Termos MeSH secundário: Arilsulfatases/genética
Arilsulfatases/metabolismo
Bacillus/citologia
Bacillus/enzimologia
Mutação
Nefelometria e Turbidimetria
Pseudomonas aeruginosa/citologia
Pseudomonas aeruginosa/enzimologia
Urato Oxidase/genética
Urato Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.7.3.3 (Urate Oxidase); EC 3.1.6.1 (Arylsulfatases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE


  3 / 1413 MEDLINE  
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[PMID]:28421414
[Au] Autor:Feng Y; Yang X; Wang D; Hu X; Chong H; Liao J; Zhan CG; Liao F
[Ad] Endereço:Unit for Analytical Probes and Protein Biotechnology, Key Laboratory of Clinical Laboratory Diagnostics of the Education Ministry, College of Laboratory Medicine, Chongqing Medical University, Chongqing, 400016, China.
[Ti] Título:Polyclonal Antibodies in Microplates to Predict the Maximum Adsorption Activities of Enzyme/Mutants from Cell Lysates.
[So] Source:Protein J;36(3):212-219, 2017 Jun.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:With microplate-immobilized polyclonal antibodies against a starting enzyme or its active mutant bearing consistent accessible epitopes, the maximum activity of an adsorbed enzyme/mutant (Vs) was predicted for comparison to recognize weakly-positive mutants. Rabbit antisera against Escherichia coli alkaline phosphatase (ECAP) were fractionated with 33% ammonium sulfate to yield crude polyclonal antibodies for conventional immobilization in 96-well microplates. The response curve of the activities of ECAP/mutant adsorbed by the immobilized polyclonal antibodies to protein quantities from a cell lysate was fit to an approximation model to predict Vs. With 0.4 µg crude polyclonal antibody for immobilization, Vs was consistent for ECAP in cell lysates bearing fourfold differences in its apparent specific activities when its abundance was greater than 0.9%. The ratio of Vs of the mutant R168K to that of ECAP was 1.5 ± 0.1 (n = 2), consistent with that of their specific activities after affinity purification. Unfortunately, the prediction of Vs with polyclonal antibodies that saturated microplate wells was ineffective to Pseudomonas aeruginosa arylsulfatase bearing less than 2% specific activity of ECAP. Therefore, with microplate-immobilized polyclonal antibodies to adsorb enzyme/mutants from cell lysates, high-throughput prediction of Vs was practical to recognize weakly-positive mutants of starting enzymes bearing fairly-high activities.
[Mh] Termos MeSH primário: Fosfatase Alcalina/química
Anticorpos/química
Arilsulfatases/química
Proteínas de Escherichia coli/química
Escherichia coli/enzimologia
Mutação de Sentido Incorreto
Pseudomonas aeruginosa/enzimologia
[Mh] Termos MeSH secundário: Fosfatase Alcalina/genética
Substituição de Aminoácidos
Animais
Arilsulfatases/genética
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Masculino
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Escherichia coli Proteins); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.1.6.1 (Arylsulfatases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-017-9716-z


  4 / 1413 MEDLINE  
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[PMID]:28107105
[Au] Autor:Pedersen M; Frandsen HL; Andersen JH
[Ad] Endereço:a National Food Institute , Technical University of Denmark , Søborg , Denmark.
[Ti] Título:Optimised deconjugation of androgenic steroid conjugates in bovine urine.
[So] Source:Food Addit Contam Part A Chem Anal Control Expo Risk Assess;34(4):482-488, 2017 Apr.
[Is] ISSN:1944-0057
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:After administration of steroids to animals the steroids are partially metabolised in the liver and kidney to phase 2 metabolites, i.e., glucuronic acid or sulphate conjugates. During analysis these conjugated metabolites are normally deconjugated enzymatically with aryl sulphatase and glucuronidase resulting in free steroids in the extract. It is well known that some sulphates are not deconjugated using aryl sulphatase; instead, for example, solvolysis can be used for deconjugation of these aliphatic sulphates. The effectiveness of solvolysis on androgenic steroid sulphates was tested with selected aliphatic steroid sulphates (boldenone sulphate, nortestosteron sulphate and testosterone sulphate), and the method was validated for analysis of androgenic steroids in bovine urine using free steroids, steroid sulphates and steroid glucuronides as standards. Glucuronidase and sulphuric acid in ethyl acetate were used for deconjugation and the extract was purified by solid-phase extraction. The final extract was evaporated to dryness, re-dissolved and analysed by LC-MS/MS.
[Mh] Termos MeSH primário: Androgênios/urina
Glucuronídeos/urina
Extração Líquido-Líquido/métodos
Esteroides/urina
Sulfatos/urina
[Mh] Termos MeSH secundário: Acetatos/química
Animais
Arilsulfatases/química
Bovinos
Cromatografia Líquida
Glucuronidase/química
Hidrólise
Nandrolona/química
Reprodutibilidade dos Testes
Ácidos Sulfúricos/química
Espectrometria de Massas em Tandem
Testosterona/análogos & derivados
Testosterona/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Androgens); 0 (Glucuronides); 0 (Steroids); 0 (Sulfates); 0 (Sulfuric Acids); 3XMK78S47O (Testosterone); 5H7I2IP58X (boldenone); 6PG9VR430D (Nandrolone); 76845O8NMZ (ethyl acetate); EC 3.1.6.1 (Arylsulfatases); EC 3.2.1.31 (Glucuronidase); O40UQP6WCF (sulfuric acid)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170308
[Lr] Data última revisão:
170308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1080/19440049.2016.1276637


  5 / 1413 MEDLINE  
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[PMID]:28055182
[Au] Autor:Dhamale OP; Lawrence R; Wiegmann EM; Shah BA; Al-Mafraji K; Lamanna WC; Lübke T; Dierks T; Boons GJ; Esko JD
[Ad] Endereço:Complex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
[Ti] Título:Arylsulfatase K is the Lysosomal 2-Sulfoglucuronate Sulfatase.
[So] Source:ACS Chem Biol;12(2):367-373, 2017 Feb 17.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The degradation of glycosaminoglycans (GAGs) involves a series of exolytic glycosidases and sulfatases that act sequentially on the nonreducing end of the polysaccharide chain. Enzymes have been cloned that catalyze all of the known linkages with the exception of the removal of the 2-O-sulfate group from 2-sulfoglucuronate, which is found in heparan sulfate and dermatan sulfate. Here, we show using synthetic disaccharide substrates that arylsulfatase K is the glucuronate-2-sulfatase. Arylsulfatase K acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate, whereas iduronate-2-sulfatase (IDS) desulfates synthetic disaccharides containing 2-sulfoiduronate but not 2-sulfoglucuronate. As arylsulfatase K has all of the properties expected of a lysosomal enzyme, we conclude that arylsulfatase K is the long sought lysosomal glucuronate-2-sulfatase, which we designate GDS.
[Mh] Termos MeSH primário: Arilsulfatases/metabolismo
Lisossomos/enzimologia
[Mh] Termos MeSH secundário: Cromatografia Líquida
Glicosaminoglicanos/metabolismo
Seres Humanos
Espectrometria de Massas
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycosaminoglycans); EC 3.1.6.1 (ARSK protein, human); EC 3.1.6.1 (Arylsulfatases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170106
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b01033


  6 / 1413 MEDLINE  
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[PMID]:27992819
[Au] Autor:Abad-Valle P; Iglesias-Jiménez E; Álvarez-Ayuso E
[Ad] Endereço:Department of Environmental Geochemistry, IRNASA (CSIC), C/Cordel de Merinas 40-52, 37008, Salamanca, Spain.
[Ti] Título:A comparative study on the influence of different organic amendments on trace element mobility and microbial functionality of a polluted mine soil.
[So] Source:J Environ Manage;188:287-296, 2017 Mar 01.
[Is] ISSN:1095-8630
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A mine soil heavily polluted with zinc and cadmium was employed to evaluate the capacity of organic amendments of different origin to simultaneously reduce soil trace element mobility and enhance soil microbial functionality. With this aim, four organic products, namely olive processing solid waste (OPSW), municipal solid waste compost (MSWC), leonardite and peat, were applied individually at different doses (0, 1, 2 and 5%) to mine soil under controlled laboratory conditions. Extraction studies and analysis of soil microbiological parameters (basal soil respiration and dehydrogenase, ß-glucosidase, urease, arylsulfatase and acid and alkaline phosphatase activities) were performed to assess the effect of such amendments on soil restoration. Their ability to decrease mine soil mobile trace element contents followed the sequence MSWC > OPSW > peat > leonardite, with the former achieving reduction levels of 78 and 73% for Zn and Cd, respectively, when applied at a dose of 5%. This amendment also showed a good performance to restore soil microbial functionality. Thus, basal soil respiration and dehydrogenase, urease and alkaline phosphatase activities experienced increases of 187, 79, 42 and 26%, respectively, when mine soil was treated with 5% MSWC. Among tested organic products, MSWC proved to be the best amendment to perform both the chemical and the microbial soil remediation.
[Mh] Termos MeSH primário: Cádmio/química
Microbiologia do Solo
Poluentes do Solo/química
Solo
Resíduos Sólidos
Zinco/química
[Mh] Termos MeSH secundário: Fosfatase Ácida/análise
Fosfatase Alcalina/análise
Arilsulfatases/análise
Proteínas de Bactérias/análise
Recuperação e Remediação Ambiental
Indústria de Processamento de Alimentos
Resíduos Industriais
Minerais
Mineração
Olea
Oxirredutases/análise
Urease/análise
beta-Glucosidase/análise
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Industrial Waste); 0 (Minerals); 0 (Soil); 0 (Soil Pollutants); 0 (Solid Waste); 0 (leonardite); 00BH33GNGH (Cadmium); EC 1.- (Oxidoreductases); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.1.3.2 (Acid Phosphatase); EC 3.1.6.1 (Arylsulfatases); EC 3.2.1.21 (beta-Glucosidase); EC 3.5.1.5 (Urease); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161220
[St] Status:MEDLINE


  7 / 1413 MEDLINE  
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[PMID]:27940339
[Au] Autor:Zhu Y; Liu H; Qiao C; Li L; Jiang Z; Xiao A; Ni H
[Ad] Endereço:College of Food and Biological Engineering, Jimei University, Xiamen 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen 361021, China; Research Center of Food Biotechnology of Xiamen City, Xiamen 361021, China; Key Laboratory of Systemic Utilization a
[Ti] Título:Characterization of an arylsulfatase from a mutant library of Pseudoalteromonas carrageenovora arylsulfatase.
[So] Source:Int J Biol Macromol;96:370-376, 2017 Mar.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A library of Pseudoalteromonas carrageenovora arylsulfatase mutants was constructed by introducing random mutagenesis using error-prone PCR. After screening, one mutant strain was obtained whose arylsulfatase had improved thermal stability. Protein sequence analysis revealed one amino acid substitution of H260L. The mutant arylsulfatase (named H260L) retained higher residual activity than wild-type enzyme (named WT) after incubation at 45, 50, 55 and 60°C for 60min. Thermal inactivation analysis showed that the half-life (t ) value at 55°C for H260L was 40.6min, while that of WT was 9.1min. When p-nitrophenyl sulfate was used as a substrate, the optimal reaction temperature and pH for the mutant enzyme were 55°C and pH 8.0, respectively. H260L was stable over the pH range of 6.0-9.0. Inhibition assay with EDTA indicated that metal ions play an important role during the catalytic process of the mutant enzyme. The desulfation ratio against agar of Gracilaria lemaneiformis was 82%.
[Mh] Termos MeSH primário: Arilsulfatases/genética
Arilsulfatases/metabolismo
Biblioteca Gênica
Mutação
Pseudoalteromonas/enzimologia
[Mh] Termos MeSH secundário: Ágar/química
Ágar/metabolismo
Arilsulfatases/química
Concentração de Íons de Hidrogênio
Modelos Moleculares
Mutagênese
Conformação Proteica
Pseudoalteromonas/genética
Sulfatos/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfates); 9002-18-0 (Agar); EC 3.1.6.1 (Arylsulfatases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE


  8 / 1413 MEDLINE  
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[PMID]:27798799
[Au] Autor:Borowik A; Wyszkowska J; Kucharski J; Bacmaga M; Tomkiel M
[Ad] Endereço:Department of Microbiology, University of Warmia and Mazury in Olsztyn, Plac Lódzki 3, 10-727, Olsztyn, Poland.
[Ti] Título:Response of microorganisms and enzymes to soil contamination with a mixture of terbuthylazine, mesotrione, and S-metolachlor.
[So] Source:Environ Sci Pollut Res Int;24(2):1910-1925, 2017 Jan.
[Is] ISSN:1614-7499
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The research objective has been to evaluate the effect, unexplored yet, of a mixture of three active ingredients of the herbicide Lumax 537.5 SE: terbuthylazine (T), mesotrione (M), and S-metolachlor (S) on counts of soil microorganisms, structure of microbial communities, activity of soil enzymes as well as the growth and development of maize. The research was based on a pot experiment established on sandy soil with pH 7.0. The herbicide was applied to soil once, in the form of liquid emulsion dosed as follows: 0.67, 13.4, 26.9, 53.8, 108, 215, and 430 mg kg of soil, converted per active substance (M + T + S). The control sample consisted of soil untreated with herbicide. The results showed that the mixture of the above active substances caused changes in values of the colony development (CD) indices of organotrophic bacteria, actinomycetes, and fungi and ecophysiological diversity (EP) indices of fungi. Changes in the ecophysiological diversity index of organotrophic bacteria and actinomycetes were small. The M + T + S mixture was a strong inhibitor of dehydrogenases, to a less degree catalase, urease, ß-glucosidase, and arylsulfatase, while being a weak inhibitor of phosphatases. The actual impact was correlated with the dosage. The M + T + S mixture inhibited the growth and development of maize. The herbicide Lumax 537.5 SE should be applied strictly in line with the regime that defines its optimum dosage. Should its application adhere to the manufacturer's instructions, the herbicide would not cause any serious disturbance in soil homeostasis. However, its excessive quantities (from 13.442 to 430.144 mg kg DM of soil) proved to be harmful to the soil environment.
[Mh] Termos MeSH primário: Acetamidas/toxicidade
Cicloexanonas/toxicidade
Herbicidas/toxicidade
Microbiologia do Solo
Poluentes do Solo/toxicidade
Triazinas/toxicidade
[Mh] Termos MeSH secundário: Actinobacteria/efeitos dos fármacos
Fosfatase Alcalina/química
Arilsulfatases/química
Azotobacter/efeitos dos fármacos
Proteínas de Bactérias/química
Catalase/química
Proteínas Fúngicas/química
Fungos/efeitos dos fármacos
Microbiota
Oxirredutases/química
Solo/química
Urease/química
Zea mays/efeitos dos fármacos
Zea mays/crescimento & desenvolvimento
Zea mays/microbiologia
beta-Glucosidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetamides); 0 (Bacterial Proteins); 0 (Cyclohexanones); 0 (Fungal Proteins); 0 (Herbicides); 0 (Soil); 0 (Soil Pollutants); 0 (Triazines); 48TR68G21T (mesotrione); EC 1.- (Oxidoreductases); EC 1.11.1.6 (Catalase); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.1.6.1 (Arylsulfatases); EC 3.2.1.21 (beta-Glucosidase); EC 3.5.1.5 (Urease); M095B391J7 (terbutylazine); X0I01K05X2 (metolachlor)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE
[do] DOI:10.1007/s11356-016-7919-z


  9 / 1413 MEDLINE  
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[PMID]:27746358
[Au] Autor:Xiao Q; Yin Q; Ni H; Cai H; Wu C; Xiao A
[Ad] Endereço:College of Food and Biological Engineering, Jimei University, Xiamen 361021, China; Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Xiamen, Fujian Province 361021, China; Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Xiamen, Fujian
[Ti] Título:Characterization and immobilization of arylsulfatase on modified magnetic nanoparticles for desulfation of agar.
[So] Source:Int J Biol Macromol;94(Pt A):576-584, 2017 Jan.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Carboxyl functioned magnetic nanoparticles (CMNPs) were prepared by a simple co-precipitation method and characterized by Fourier transform infrared spedtroscopy and scanning electron microscope. The prepared CMNPs were used for covalent immobilization of the arylsulfatase which could be applied in desulfation of agar. The optimal immobilizaion conditions were obtained as follows: glutaraldehyde concentration 1.0% (v/v), cross-linking time 3h, immobilization time 3h, immobilization temperature 5°C and enzyme dose 0.62U. Increase in properties of the arylsulfatase such as optimum temperature and pH was observed after immobilization. Immobilization led to increased tolerance of enzyme to some metal ions, inhibitors and detergents. The K and k of the immobilized enzyme for hydrolysis of p-NPS at pH 7.5 and at 50°C were determined to be 0.89mmol/L and 256.91s , respectively. The relative desulfuration rates of immobilized arylsulfatase maintained 61.7% of its initial desulfuration rates after seven cycles. After the reaction of agar with immobilized arylsulfatase for 90min at 50°C, 46% of the sulfate in the agar was removed. These results showed that the immobilization of arylsulfatase onto CMNPs is an efficient and simple way for preparation of stable arylsulfatase and have a great potential for application in enzymatic desulfation of agar.
[Mh] Termos MeSH primário: Ágar/química
Arilsulfatases/química
Proteínas de Bactérias/química
Enzimas Imobilizadas/química
Nanopartículas de Magnetita/química
[Mh] Termos MeSH secundário: Precipitação Química
Reagentes para Ligações Cruzadas/química
Estabilidade Enzimática
Reutilização de Equipamento
Óxido Ferroso-Férrico/química
Glutaral/química
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Nanopartículas de Magnetita/ultraestrutura
Nitrobenzenos/química
Proteínas Recombinantes/química
Sulfatos/química
Temperatura Ambiente
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cross-Linking Reagents); 0 (Enzymes, Immobilized); 0 (Magnetite Nanoparticles); 0 (Nitrobenzenes); 0 (Recombinant Proteins); 0 (Sulfates); 1080-04-2 (4-nitrophenyl sulfate); 9002-18-0 (Agar); EC 3.1.6.1 (Arylsulfatases); T3C89M417N (Glutaral); XM0M87F357 (Ferrosoferric Oxide)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161018
[St] Status:MEDLINE


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[PMID]:27654655
[Au] Autor:Stressler T; Seitl I; Kuhn A; Fischer L
[Ad] Endereço:Institute of Food Science and Biotechnology, Department of Biotechnology and Enzyme Science, University of Hohenheim, Garbenstr. 25, 70599, Stuttgart, Germany. t.stressler@uni-hohenheim.de.
[Ti] Título:Detection, production, and application of microbial arylsulfatases.
[So] Source:Appl Microbiol Biotechnol;100(21):9053-9067, 2016 Nov.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Arylsulfatases are enzymes which catalyze the hydrolysis of arylsulfate ester bonds to release a free sulfonate. They are widespread in nature and are found in microorganisms, most animal and human tissues, and plant seeds. However, this review focuses on arylsulfatases from microbial origin and gives an overview of different assays and substrates used to determine the arylsulfatase activity. Furthermore, the production of microbial arylsulfatases using wild-type organisms as well as the recombinant production using Escherichia coli and Kluyveromyces lactis as expression hosts is discussed. Finally, various potential applications of these enzymes are reviewed.
[Mh] Termos MeSH primário: Arilsulfatases/análise
Arilsulfatases/metabolismo
Bactérias/enzimologia
Fungos/enzimologia
[Mh] Termos MeSH secundário: Arilsulfatases/genética
Bactérias/genética
Expressão Gênica
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 3.1.6.1 (Arylsulfatases)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160923
[St] Status:MEDLINE



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