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[PMID]:29231937
[Au] Autor:Ugrinic M; Zambrano A; Berger S; Mann S; Tang TD; deMello A
[Ad] Endereço:Department of Chemistry & Applied Biosciences, ETH Zurich, Vladimir Prelog Weg 1, 8093 Zurich, Switzerland. andrew.demello@chem.ethz.ch.
[Ti] Título:Microfluidic formation of proteinosomes.
[So] Source:Chem Commun (Camb);54(3):287-290, 2018 Jan 02.
[Is] ISSN:1364-548X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Herein we describe a novel microfluidic method for the generation of proteinosome micro-droplets, based on bovine serum albumin and glucose oxidase conjugated to PNIPAAm chains. The size of such water-in-oil droplets is regulated via control of the input reagent flow rate, with generated proteinosome populations exhibiting narrower size distributions than those observed when using standard bulk methodologies. Importantly, proteinosomes transferred from an oil to an aqueous-environment remain intact, become fully hydrated and exhibit an increase in average size. Moreover, functional proteinosomes prepared via microfluidics exhibit lower K values and higher enzymatic activities than proteinosomes produced by bulk methodologies.
[Mh] Termos MeSH primário: Células Artificiais/química
Glucose Oxidase/química
Soroalbumina Bovina/química
[Mh] Termos MeSH secundário: Resinas Acrílicas/química
Animais
Bovinos
Fluoresceína-5-Isotiocianato/química
Peroxidase do Rábano Silvestre/química
Microfluídica
Tamanho da Partícula
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acrylic Resins); 25189-55-3 (poly-N-isopropylacrylamide); 27432CM55Q (Serum Albumin, Bovine); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.- (Horseradish Peroxidase); I223NX31W9 (Fluorescein-5-isothiocyanate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1039/c7cc08466h


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[PMID]:28471002
[Au] Autor:Cecchini MM; Reale S; Manini P; d'Ischia M; De Angelis F
[Ad] Endereço:Department of Physical and Chemical Sciences, University of L'Aquila, Via Vetoio, Coppito, L'Aquila, Italy.
[Ti] Título:Modeling Fungal Melanin Buildup: Biomimetic Polymerization of 1,8-Dihydroxynaphthalene Mapped by Mass Spectrometry.
[So] Source:Chemistry;23(33):8092-8098, 2017 Jun 12.
[Is] ISSN:1521-3765
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Due to the emerging biomedical relevance and technological potential of fungal melanins, and prompted by the virtual lack of information about their structural arrangement, an optimized synthetic protocol has been devised for a potential structural model of Ascomyces allomelanin through enzyme-catalyzed oxidative polymerization of 1,8-dihydroxynaphthalene (1,8-DHN). Electrospray ionization mass spectrometry (ESI-MS) measurements of freshly synthesized DHN-polymer recorded in the negative ion mode allowed detection of oligomers up to m/z 4000, separated by 158 Da, corresponding to the in-chain DHN-unit. The dominant peaks were assigned to singly-charged distribution, up to 23 repeating units, whereas a doubly charged polymer distribution was also detectable. Chemical derivatization, ultra-performance liquid chromatography (UPLC)-ESI MS, and MS/MS data confirmed that oxidative polymerization of 1,8-DHN proceeds through C-C coupling of the naphthalene rings. The new insights reported here into synthetic 1,8-DHN oligomers/polymers as a mimic of fungal melanins may guide novel interesting advances and applications in the field of biomimetic functional materials.
[Mh] Termos MeSH primário: Materiais Biomiméticos/química
Proteínas Fúngicas/metabolismo
Fungos/metabolismo
Melaninas/metabolismo
Naftóis/química
[Mh] Termos MeSH secundário: Biocatálise
Materiais Biomiméticos/metabolismo
Cromatografia Líquida de Alta Pressão
Proteínas Fúngicas/química
Peroxidase do Rábano Silvestre/metabolismo
Melaninas/química
Oxirredução
Polimerização
Espectrometria de Massas por Ionização por Electrospray
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Melanins); 0 (Naphthols); 569-42-6 (1,8-dihydroxynaphthalene); EC 1.11.1.- (Horseradish Peroxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1002/chem.201701951


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[PMID]:28467664
[Au] Autor:Gamella M; Privman M; Bakshi S; Melman A; Katz E
[Ad] Endereço:Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, NY, 13699-5810, USA.
[Ti] Título:DNA Release from Fe -Cross-Linked Alginate Films Triggered by Logically Processed Biomolecular Signals: Integration of Biomolecular Computing and Actuation.
[So] Source:Chemphyschem;18(13):1811-1821, 2017 Jul 05.
[Is] ISSN:1439-7641
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Signal-controlled release of DNA from Fe -cross-linked alginate hydrogel electrochemically deposited on an electrode surface was studied. The multiple input signals were logically processed with the help of the enzyme-biocatalyzed reactions. Boolean logic gates, OR, AND, INH, were realized with the biocatalytic reactions performed by the enzymes entrapped in the alginate film. Hydrogen peroxide produced by the enzymatic reactions resulted in the degradation of the alginate hydrogel and DNA release. The alginate degradation was facilitated by the formation of free radicals in the Fenton-type reaction catalyzed by iron cations cross-linking the alginate hydrogel. The studied approach is versatile and can be adapted to various chemical signals processed by various enzymes with differently implemented Boolean logic. This work illustrates a novel concept of functional integration of biomolecular computing and actuation.
[Mh] Termos MeSH primário: Alginatos/química
Computadores Moleculares
Reagentes para Ligações Cruzadas/química
DNA/metabolismo
Compostos Férricos/química
Lógica
[Mh] Termos MeSH secundário: Animais
Biocatálise
DNA/química
Esterases/química
Esterases/metabolismo
Glucose Oxidase/química
Glucose Oxidase/metabolismo
Ácido Glucurônico/química
Ácidos Hexurônicos/química
Peroxidase do Rábano Silvestre/química
Peroxidase do Rábano Silvestre/metabolismo
Lactato Desidrogenases/química
Lactato Desidrogenases/metabolismo
Oxigenases de Função Mista/química
Oxigenases de Função Mista/metabolismo
Nanopartículas/química
Nanopartículas/metabolismo
Dióxido de Silício/química
Dióxido de Silício/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alginates); 0 (Cross-Linking Reagents); 0 (Ferric Compounds); 0 (Hexuronic Acids); 7631-86-9 (Silicon Dioxide); 8A5D83Q4RW (Glucuronic Acid); 8C3Z4148WZ (alginic acid); 9007-49-2 (DNA); EC 1.- (Mixed Function Oxygenases); EC 1.1.- (Lactate Dehydrogenases); EC 1.1.3.4 (Glucose Oxidase); EC 1.11.1.- (Horseradish Peroxidase); EC 1.13.12.4 (lactate 2-monooxygenase); EC 3.1.- (Esterases)
[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:170504
[St] Status:MEDLINE
[do] DOI:10.1002/cphc.201700301


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[PMID]:27770413
[Au] Autor:Stine KJ; Jefferson K; Shulga OV
[Ad] Endereço:Department of Chemistry and Biochemistry, Center for Nanoscience, University of Missouri-Saint Louis, One University Boulevard, Saint Louis, MO, 63121-4400, USA. kstine@umsl.edu.
[Ti] Título:Nanoporous Gold for Enzyme Immobilization.
[So] Source:Methods Mol Biol;1504:37-60, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nanoporous gold (NPG) is a material of emerging interest for immobilization of biomolecules, especially enzymes. The material provides a high surface area form of gold that is suitable for physisorption or for covalent modification by self-assembled monolayers. The material can be used as a high surface area electrode and with immobilized enzymes can be used for amperometric detection schemes. NPG can be prepared in a variety of formats from alloys containing between 20 and 50 % atomic composition of gold and less noble element(s) by dealloying procedures. Materials resembling NPG can be prepared by hydrothermal and electrodeposition methods. Related high surface area gold structures have been prepared using templating approaches. Covalent enzyme immobilization can be achieved by first forming a self-assembled monolayer on NPG bearing a terminal reactive functional group followed by conjugation to the enzyme through amide linkages to lysine residues. Enzymes can also be entrapped by physisorption or immobilized by electrostatic interactions.
[Mh] Termos MeSH primário: Enzimas Imobilizadas/química
Ouro/química
Nanoporos/ultraestrutura
[Mh] Termos MeSH secundário: Acetilcolinesterase/química
Animais
Técnicas Biossensoriais
Técnicas Eletroquímicas
Eletrodos
Estabilidade Enzimática
Glucose Oxidase/química
Peroxidase do Rábano Silvestre/química
Seres Humanos
Imunoconjugados/química
Lacase/química
Complexo de Proteína do Fotossistema I/química
Porosidade
Spinacia oleracea/enzimologia
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Immunoconjugates); 0 (Photosystem I Protein Complex); 7440-57-5 (Gold); EC 1.1.3.4 (Glucose Oxidase); EC 1.10.3.2 (Laccase); EC 1.11.1.- (Horseradish Peroxidase); EC 3.1.1.7 (Acetylcholinesterase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


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[PMID]:28741467
[Au] Autor:Kubizek F; Eggenreich B; Spadiut O
[Ad] Endereço:Vienna University of Technology, Institute of Chemical Engineering, Research Area Biochemical Engineering, Gumpendorfer Strasse 1a, 1060 Vienna. Austria.
[Ti] Título:Status Quo in Antibody-Drug Conjugates - Can Glyco- Enzymes Solve the Current Challenges?
[So] Source:Protein Pept Lett;24(8):686-695, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Over the last years, a novel class of anti-cancer drugs named antibody-drug conjugates (ADCs) has been developed. Due to their limited off-target toxicity but highly potent cytotoxicity at tumor sites, ADCs have proven to be a good alternative to ordinary cancer treatment, such as chemotherapy or combination therapy. Numerous enhancements in antibody-drug engineering led to highly potent tumor targeting drugs with a wide therapeutic window. Two ADCs (Brentuximab vedotin and Trastuzumab emtansine) are already on the market and many others are in clinical trials. However, unstable linkers, low drug potency and unwanted bystander-effects are only some of the drawbacks of ADCs. Enzymes used in combination with prodrugs happen to be a promising alternative. The glyco-enzyme horseradish peroxidase (HRP) has proven to activate the hormone indole-3-acetic acid (IAA) to a highly potent cytotoxic drug. This combination of IAA and HRP has been investigated for the use in strategies such as gene-directed enzyme prodrug therapy (GDEPT) and antibody-directed enzyme prodrug therapy (ADEPT). This article reviews the current state of research in ADC engineering and describes the potential major enhancements through use of glycoenzymes in combination with a prodrug.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/biossíntese
Antineoplásicos Imunológicos/uso terapêutico
Imunoconjugados/uso terapêutico
Maitansina/análogos & derivados
Terapia de Alvo Molecular
Neoplasias/tratamento farmacológico
Trastuzumab/uso terapêutico
[Mh] Termos MeSH secundário: Anticorpos Monoclonais/uso terapêutico
Antineoplásicos Imunológicos/metabolismo
Ensaios Clínicos como Assunto
Desenho de Drogas
Glicoconjugados/síntese química
Glicoconjugados/uso terapêutico
Peroxidase do Rábano Silvestre/metabolismo
Peroxidase do Rábano Silvestre/uso terapêutico
Seres Humanos
Imunoconjugados/química
Ácidos Indolacéticos/metabolismo
Maitansina/biossíntese
Maitansina/uso terapêutico
Neoplasias/genética
Neoplasias/metabolismo
Neoplasias/patologia
Pró-Fármacos/síntese química
Pró-Fármacos/uso terapêutico
Trastuzumab/biossíntese
Moduladores de Tubulina/síntese química
Moduladores de Tubulina/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Antineoplastic Agents, Immunological); 0 (Glycoconjugates); 0 (Immunoconjugates); 0 (Indoleacetic Acids); 0 (Prodrugs); 0 (Tubulin Modulators); 14083FR882 (Maytansine); 6U1S09C61L (indoleacetic acid); 7XL5ISS668 (brentuximab vedotin); EC 1.11.1.- (Horseradish Peroxidase); P188ANX8CK (Trastuzumab); SE2KH7T06F (ado-trastuzumab emtansine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170724105211


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[PMID]:28843840
[Au] Autor:Mahfoudi R; Djeridane A; Benarous K; Gaydou EM; Yousfi M
[Ad] Endereço:Laboratoire des Sciences fondamentales, Université Amar Telidji, Laghouat BP37G, Laghouat, Algeria; Laboratoire des Sciences chimiques et physiques appliquées, ENS de Laghouat, BP 4033 Laghouat, Algeria.
[Ti] Título:Structure-activity relationships and molecular docking of thirteen synthesized flavonoids as horseradish peroxidase inhibitors.
[So] Source:Bioorg Chem;74:201-211, 2017 Oct.
[Is] ISSN:1090-2120
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For the first time, the structure-activity relationships of thirteen synthesized flavonoids have been investigated by evaluating their ability to modulate horseradish peroxidase (HRP) catalytic activity. Indeed, a modified spectrophotometrically method was carried out and optimized using 4-methylcatechol (4-MC) as peroxidase co-substrate. The results show that these flavonoids exhibit a great capacity to inhibit peroxidase with Ki values ranged from 0.14±0.01 to 65±0.04mM. Molecular docking has been achieved using Auto Dock Vina program to discuss the nature of interactions and the mechanism of inhibition. According to the docking results, all the flavonoids have shown great binding affinity to peroxidase. These molecular modeling studies suggested that pyran-4-one cycle acts as an inhibition key for peroxidase. Therefore, potent peroxidase inhibitors are flavonoids with these structural requirements: the presence of the hydroxyl (OH) group in 7, 5 and 4' positions and the absence of the methoxy (O-CH ) group. Apigenin contributed better in HRP inhibitory activity. The present study has shown that the studied flavonoids could be promising HRP inhibitors, which can help in developing new molecules to control thyroid diseases.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Inibidores Enzimáticos/farmacologia
Flavonoides/farmacologia
Peroxidase do Rábano Silvestre/antagonistas & inibidores
Simulação de Acoplamento Molecular
[Mh] Termos MeSH secundário: Antioxidantes/síntese química
Antioxidantes/química
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Flavonoides/síntese química
Flavonoides/química
Peroxidase do Rábano Silvestre/metabolismo
Estrutura Molecular
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Enzyme Inhibitors); 0 (Flavonoids); EC 1.11.1.- (Horseradish Peroxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170828
[St] Status: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


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[PMID]:28712944
[Au] Autor:Yuan Y; Li S; Xue Y; Liang J; Cui L; Li Q; Zhou S; Huang Y; Li G; Zhao Y
[Ad] Endereço:Department of Clinical Laboratory, The People's Hospital of Guangxi Zhuang Autonomous Region, Nanning, Guangxi 530021, China.
[Ti] Título:A Fe O @Au-basedpseudo-homogeneous electrochemical immunosensor for AFP measurement using AFP antibody-GNPs-HRP as detection probe.
[So] Source:Anal Biochem;534:56-63, 2017 Oct 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, a Fe O @Au-based pseudo-homogeneous electrochemical immunosensor was prepared for detection of alpha fetoprotein (AFP), a well-known hepatocellular carcinoma biomarker. The primary antibody (Ab1) was immobilized on Fe O @Au NPs as the capture probe. Horseradish peroxidase (HRP) and secondary antibody (Ab2) were conjugated on gold nanoparticles (GNPs) through electrostatic adsorption to form signal-amplifying labels. In the presence of AFP, a sandwich immunocomplex was formed via specific recognition of antigen-antibody in a Fe O @Au-basedpseudo-homogeneousreaction system. After the immunocomplex was captured to the surface of magnetic glassy carbon electrode (MGCE), the labeling HRP catalyzed the decomposition of H O , resulting in a substantial current for the quantitative detection of AFP. The amperometric (i-t) method was employed to record the response signal of the immunosensor based on the catalysis of the immobilized HRP toward the reduction of H O with hydroquinone (HQ) as the redox mediator. Under the optimal conditions, the amperometric current response presented a linear relationship with AFP concentration over the range of 20 ng/mL-100 ng/mLwith a correlation coefficient of 0.9940, and the detection limit was 0.64 ng/mL at signal/noise [S/N] = 3. Moreover, the electrochemical immunosensor exhibited higher anti-interference ability, acceptable reproducibility and long-term stability for AFP detection.
[Mh] Termos MeSH primário: Anticorpos/química
Óxido Ferroso-Férrico/química
Ouro/química
Peroxidase do Rábano Silvestre/química
Sondas Moleculares/química
alfa-Fetoproteínas/análise
[Mh] Termos MeSH secundário: Técnicas Eletroquímicas
Eletrodos
Peroxidase do Rábano Silvestre/metabolismo
Imunoensaio
Nanopartículas Metálicas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Molecular Probes); 0 (alpha-Fetoproteins); 7440-57-5 (Gold); EC 1.11.1.- (Horseradish Peroxidase); XM0M87F357 (Ferrosoferric Oxide)
[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:170718
[St] Status:MEDLINE


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[PMID]:28692846
[Au] Autor:Tallapragada SD; Layek K; Mukherjee R; Mistry KK; Ghosh M
[Ad] Endereço:National Institute of Technology, M. G. Avenue, Durgapur 713209, India.
[Ti] Título:Development of screen-printed electrode based immunosensor for the detection of HER2 antigen in human serum samples.
[So] Source:Bioelectrochemistry;118:25-30, 2017 Dec.
[Is] ISSN:1878-562X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In this study, an immunosensor based on screen-printed electrode (SPE) has been developed for the detection of Human Epidermal Growth Factor Receptor-2 (HER2) antigen. The SPEs were fabricated and a sandwich enzyme linked immunosorbent assay (ELISA) format was followed for the construction of the immunosensor. The capture antibody (mouse anti-human ErbB2) was coated onto the electrode surface without any prior surface modification, followed by the addition of recombinant human HER2 antigen. Biotinylated goat anti-human ErbB2 was used as the detection antibody which was linked to streptavidin conjugated horseradish peroxidase (HRP). 3,3',5,5'-tetramethylbenzidine (TMB) was used as the substrate. The redox reaction was measured using cyclic voltammetry at scan rate of 50mV/s for the quantification of the antigen in solution. The biotin-avidin chemistry enabled the accurate detection of the antigen in nanogram levels. The amperometric signal obtained increased linearly with increase in the HER2 concentration and two-fold linear range was obtained between 5ng/ml-20ng/ml and 20-200ng/ml respectively. The limit of detection (LOD) and the limit of quantification (LOQ) of this immunosensor were found to be 4ng/ml and 5ng/ml respectively. The detection of HER2 in the serum samples of invasive and non-invasive breast cancer patients has been realized.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/instrumentação
Análise Química do Sangue/instrumentação
Ensaio de Imunoadsorção Enzimática/instrumentação
Impressão
Receptor ErbB-2/sangue
[Mh] Termos MeSH secundário: Anticorpos Imobilizados/química
Anticorpos Imobilizados/imunologia
Benzidinas/química
Eletroquímica
Eletrodos
Peroxidase do Rábano Silvestre/química
Peroxidase do Rábano Silvestre/metabolismo
Seres Humanos
Limite de Detecção
Receptor ErbB-2/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Immobilized); 0 (Benzidines); 3B3T5CB8EO (3,3',5,5'-tetramethylbenzidine); EC 1.11.1.- (Horseradish Peroxidase); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170927
[Lr] Data última revisão:
170927
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE


  10 / 14768 MEDLINE  
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[PMID]:28674329
[Au] Autor:Morita M; Tani M; Honjo T
[Ad] Endereço:Sapporo Campus, Hokkaido University of Education.
[Ti] Título:Decomposition of Fatty Acid and Detergency Using a System Combining Horseradish Peroxidase and p-Iodophenol.
[So] Source:J Oleo Sci;66(7):797-799, 2017.
[Is] ISSN:1347-3352
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The reactivity and detergency of a horseradish peroxidase reaction system with oleic acid, a non-hydrogen donor used as a soil component, were studied. Under a coexistent system of horseradish peroxidase and p-iodophenol, oleic acid decomposed quickly. In addition, because the coexistence of p-iodophenol provided detergency, a new function of horseradish peroxidase was shown.
[Mh] Termos MeSH primário: Detergentes/química
Ácidos Graxos/química
Peroxidase do Rábano Silvestre/química
Iodobenzenos/química
Ácido Oleico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Detergents); 0 (Fatty Acids); 0 (Iodobenzenes); 2UMI9U37CP (Oleic Acid); 540-38-5 (4-iodophenol); EC 1.11.1.- (Horseradish Peroxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.5650/jos.ess17095



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