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  1 / 20325 MEDLINE  
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[PMID]:29373594
[Au] Autor:Grimm I; Dumke J; Dreier J; Knabbe C; Vollmer T
[Ad] Endereço:Institut für Laboratoriums- und Transfusionsmedizin, Herz- und Diabeteszentrum Nordrhein-Westfalen, Universitätsklinikum der Ruhr-Universität Bochum, Bad Oeynhausen, Germany.
[Ti] Título:Biofilm formation and transcriptome analysis of Streptococcus gallolyticus subsp. gallolyticus in response to lysozyme.
[So] Source:PLoS One;13(1):e0191705, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Streptococcus gallolyticus subsp. gallolyticus is a commensal bacterium of the human gastrointestinal tract, and a pathogen causing infective endocarditis and other biofilm-associated infections via exposed collagen. This study focuses on the characterization of the biofilm formation and collagen adhesion of S. gallolyticus subsp. gallolyticus under different conditions. In this study, it has been observed that the isolate UCN 34 is resistant to 20 mg/ml lysozyme in BHI medium, whereas the strain BAA-2069 builds more biofilm in the presence of lysozyme compared to in a control of BHI without lysozyme. A transcriptome analysis with whole genome microarrays of these two isolates in BHI medium with lysozyme compared to control without lysozyme revealed changes in gene expression levels. In the isolate BAA-2069, 67 genes showed increased expression in the presence of lysozyme, while in the isolate UCN 34, 165 genes showed increased expression and 30 genes showed decreased expression through lysozyme treatment. Products of genes which were higher expressed are in involved in transcription and translation, in cell-wall modification, in hydrogen peroxide resistance and in bacterial immunity. Furthermore, the adhesion ability of different strains of S. gallolyticus subsp. gallolyticus to collagen type I and IV was analyzed. Thereby, we compared the adhesion of 46 human isolates with 23 isolates from animals. It was shown that the adhesion ability depends significantly on whether the isolate was isolated from human or animal. For example, high adhesion ability was observed for strain UCN 34 isolated from an infective endocarditis patient, whereas strain DSM 16831 isolated from koala feces adhered only marginally to collagen. Full genome microarray analysis of these two strains revealed strain-dependent gene expression due to adhesion. The expression of 25 genes of a transposon and 15 genes of a phage region in strain DSM 16831 were increased, which corresponds to horizontal gene transfer. Adherence to collagen in strain UCN 34 led to higher expression of 27 genes and lower expression of 31 genes. This was suggestive of a change in nutrient uptake.
[Mh] Termos MeSH primário: Biofilmes
Muramidase/metabolismo
Streptococcus gallolyticus subspecies gallolyticus/metabolismo
Transcriptoma
[Mh] Termos MeSH secundário: Streptococcus gallolyticus subspecies gallolyticus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.17 (Muramidase)
[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:180127
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191705


  2 / 20325 MEDLINE  
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[PMID]:29328338
[Au] Autor:Soler MA; Fortuna S; de Marco A; Laio A
[Ad] Endereço:SISSA, Via Bonomea 265, I-34136 Trieste, Italy. miguelangel.solerbastida@sissa.it fortuna@sissa.it.
[Ti] Título:Binding affinity prediction of nanobody-protein complexes by scoring of molecular dynamics trajectories.
[So] Source:Phys Chem Chem Phys;20(5):3438-3444, 2018 Jan 31.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nanobodies offer a viable alternative to antibodies for engineering high affinity binders. Their small size has an additional advantage: it allows exploiting computational protocols for optimizing their biophysical features, such as the binding affinity. The efficient prediction of this quantity is still considered a daunting task especially for modelled complexes. We show how molecular dynamics can successfully assist in the binding affinity prediction of modelled nanobody-protein complexes. The approximate initial configurations obtained by in silico design must undergo large rearrangements before achieving a stable conformation, in which the binding affinity can be meaningfully estimated. The scoring functions developed for the affinity evaluation of crystal structures will provide accurate estimates for modelled binding complexes if the scores are averaged over long finite temperature molecular dynamics simulations.
[Mh] Termos MeSH primário: Complexo Antígeno-Anticorpo/química
Simulação de Dinâmica Molecular
Proteínas/imunologia
Anticorpos de Cadeia Única/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Afinidade de Anticorpos
Complexo Antígeno-Anticorpo/metabolismo
Seres Humanos
Muramidase/química
Muramidase/imunologia
Estrutura Terciária de Proteína
Proteínas/química
Receptor ErbB-2/química
Receptor ErbB-2/metabolismo
Alinhamento de Sequência
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Proteins); 0 (Single-Chain Antibodies); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 3.2.1.17 (Muramidase)
[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:180113
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp08116b


  3 / 20325 MEDLINE  
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[PMID]:29309999
[Au] Autor:Millan S; Satish L; Bera K; Konar M; Sahoo H
[Ad] Endereço:Department of Chemistry, National Institute of Technology (NIT), Rourkela, Odisha, India.
[Ti] Título:Exploring the effect of 5-Fluorouracil on conformation, stability and activity of lysozyme by combined approach of spectroscopic and theoretical studies.
[So] Source:J Photochem Photobiol B;179:23-31, 2018 Feb.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:In this present work, a detailed investigation of the effect of an anticancer drug, 5-Fluorouracil (5-FU), on conformation, stability and activity of lysozyme (Lyz) was reported. The interaction between Lyz and 5-FU was reflected in terms of intrinsic fluorescence quenching and change in secondary structure of Lyz. The mode of quenching mechanism involved was evaluated by the steady-state and time-resolved fluorescence measurements. Synchronous and Circular Dichroism (CD) results revealed the conformational changes induced in Lyz upon complexation with 5-FU. Additionally, the effect of temperature and chemical denaturant on the stability of Lyz-5FU complex was carried out. As well as the activity of Lyz in the absence and presence of 5-FU were measured using Micrococcus luteus strain. To support our experimental findings, in vitro interaction between Lyz and 5-FU was done by theoretical studies. The current study will provide a better understanding on the nature of the interactions possible between proteins and drug molecules, which might create a bench mark in medical science in terms of the toxic effect or biological benefits of drug molecules on protein structure and conformation.
[Mh] Termos MeSH primário: Fluoruracila/metabolismo
Modelos Moleculares
Muramidase/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Fluoruracila/química
Guanidina/química
Muramidase/química
Ligação Proteica
Desnaturação Proteica
Estabilidade Proteica
Estrutura Secundária de Proteína
Espectrometria de Fluorescência
Temperatura Ambiente
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.17 (Muramidase); JU58VJ6Y3B (Guanidine); U3P01618RT (Fluorouracil)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  4 / 20325 MEDLINE  
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[PMID]:28470607
[Au] Autor:Britton J; Smith JN; Raston CL; Weiss GA
[Ad] Endereço:Department of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, CA, 92697-2025, USA.
[Ti] Título:Protein Folding Using a Vortex Fluidic Device.
[So] Source:Methods Mol Biol;1586:211-220, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Essentially all biochemistry and most molecular biology experiments require recombinant proteins. However, large, hydrophobic proteins typically aggregate into insoluble and misfolded species, and are directed into inclusion bodies. Current techniques to fold proteins recovered from inclusion bodies rely on denaturation followed by dialysis or rapid dilution. Such approaches can be time consuming, wasteful, and inefficient. Here, we describe rapid protein folding using a vortex fluidic device (VFD). This process uses mechanical energy introduced into thin films to rapidly and efficiently fold proteins. With the VFD in continuous flow mode, large volumes of protein solution can be processed per day with 100-fold reductions in both folding times and buffer volumes.
[Mh] Termos MeSH primário: Hidrodinâmica
Muramidase/química
Dobramento de Proteína
[Mh] Termos MeSH secundário: Animais
Tampões (Química)
Galinhas
Desenho de Equipamento
Escherichia coli/genética
Expressão Gênica
Muramidase/genética
Física/instrumentação
Desnaturação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Buffers); 0 (Recombinant Proteins); EC 3.2.1.- (hen egg lysozyme); EC 3.2.1.17 (Muramidase)
[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:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_13


  5 / 20325 MEDLINE  
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[PMID]:29357364
[Au] Autor:Seraj Z; Seyedarabi A; Saboury AA; Habibi-Rezaei M; Ahmadian S; Ghasemi A
[Ad] Endereço:Department of Biochemistry, Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
[Ti] Título:Unraveling the novel effects of aroma from small molecules in preventing hen egg white lysozyme amyloid fibril formation.
[So] Source:PLoS One;13(1):e0189754, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study investigated for the first time the molecular effectiveness of 'aroma' from three small molecules including a phenol (phenyl ethyl alcohol; PEA) and an aldehyde (cinnamaldehyde; Cin) both containing an aromatic ring, and a diamine (N,N,N,N'- Tetramethylethylenediamine; TEMED) at two different amounts (small; S and large; L) in preventing hen egg white lysozyme (HEWL) amyloid fibril formation using Thioflavin T and Nile red fluorescence assays, circular dichroism spectroscopy, SDS-polyacrylamide gel electrophoresis, atomic force microscopy, dynamic light scattering and HEWL activity test. Interestingly, the results revealed that (1) the aroma of PEA, identified as an active constituent of Rosa damascena, prevented fibril formation since PEA-L was able to trap the oligomeric form of HEWL in contrast to PEA-S where protofibrils but not mature fibrils were formed; (2) Cin, previously shown to prevent fibril formation in the liquid form, was also shown to do so in the aroma form by producing protofibrils and not mature fibrils in both Cin- L and Cin-S aroma forms and (3) the aroma of TEMED-L was able to retain HEWL's native structure completely and prevented both aggregation and fibril formation, while TEMED-S prevented HEWL fibril formation and instead directed the pathway towards amorphous aggregate formation. Furthermore, the ability to trap oligomeric species (by PEA-L aroma) is of great importance for further research as it provides routes for preventing the formation of toxic oligomeric intermediates along the fibrillation pathway. Last but not least, the novelty of this in vitro study on the effect of aroma at the molecular level with a unique experimental set-up using HEWL as a model protein in assessing amyloid fibril formation paves the way for more and detailed studies on the importance of aroma producing molecules and their effects.
[Mh] Termos MeSH primário: Amiloide/metabolismo
Clara de Ovo
Muramidase/metabolismo
Odorantes
[Mh] Termos MeSH secundário: Animais
Galinhas
Dicroísmo Circular
Eletroforese em Gel de Poliacrilamida
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amyloid); EC 3.2.1.17 (Muramidase)
[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:180123
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189754


  6 / 20325 MEDLINE  
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[PMID]:29288052
[Au] Autor:Shukla N; Pomarico E; Hecht CJS; Taylor EA; Chergui M; Othon CM
[Ad] Endereço:Department of Physics, Wesleyan University, Middletown, CT 06457, USA.
[Ti] Título:Hydrophobic interactions of sucralose with protein structures.
[So] Source:Arch Biochem Biophys;639:38-43, 2018 02 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sucralose is a commonly employed artificial sweetener that appears to destabilize protein native structures. This is in direct contrast to the bio-preservative nature of its natural counterpart, sucrose, which enhances the stability of biomolecules against environmental stress. We have further explored the molecular interactions of sucralose as compared to sucrose to illuminate the origin of the differences in their bio-preservative efficacy. We show that the mode of interactions of sucralose and sucrose in bulk solution differ subtly through the use of hydration dynamics measurement and computational simulation. Sucralose does not appear to disturb the native state of proteins for moderate concentrations (<0.2 M) at room temperature. However, as the concentration increases, or in the thermally stressed state, sucralose appears to differ in its interactions with protein leading to the reduction of native state stability. This difference in interaction appears weak. We explored the difference in the preferential exclusion model using time-resolved spectroscopic techniques and observed that both molecules appear to be effective reducers of bulk hydration dynamics. However, the chlorination of sucralose appears to slightly enhance the hydrophobicity of the molecule, which reduces the preferential exclusion of sucralose from the protein-water interface. The weak interaction of sucralose with hydrophobic pockets on the protein surface differs from the behavior of sucrose. We experimentally followed up upon the extent of this weak interaction using isothermal titration calorimetry (ITC) measurements. We propose this as a possible origin for the difference in their bio-preservative properties.
[Mh] Termos MeSH primário: Interações Hidrofóbicas e Hidrofílicas
Modelos Químicos
Muramidase/química
Sacarose/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Galinhas
Sacarose/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
57-50-1 (Sucrose); 96K6UQ3ZD4 (trichlorosucrose); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


  7 / 20325 MEDLINE  
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[PMID]:29199979
[Au] Autor:Quirnheim Pais D; Rathmann B; Koepke J; Tomova C; Wurzinger P; Thielmann Y
[Ad] Endereço:Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.
[Ti] Título:A standardized technique for high-pressure cooling of protein crystals.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 12):997-1006, 2017 Dec 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cryogenic temperatures slow down secondary radiation damage during data collection from macromolecular crystals. In 1973, cooling at high pressure was identified as a method for cryopreserving crystals in their mother liquor [Thomanek et al. (1973). Acta Cryst. A29, 263-265]. Results from different groups studying different crystal systems indicated that the approach had merit, although difficulties in making the process work have limited its widespread use. Therefore, a simplified and reliable technique has been developed termed high-pressure cooling (HPC). An essential requirement for HPC is to protect crystals in capillaries. These capillaries form part of new sample holders with SPINE standard dimensions. Crystals are harvested with the capillary, cooled at high pressure (220 MPa) and stored in a cryovial. This system also allows the usage of the standard automation at the synchrotron. Crystals of hen egg-white lysozyme and concanavalin A have been successfully cryopreserved and yielded data sets to resolutions of 1.45 and 1.35 Å, respectively. Extensive work has been performed to define the useful working range of HPC in capillaries with 250 µm inner diameter. Three different 96-well crystallization screens that are most frequently used in our crystallization facility were chosen to study the formation of amorphous ice in this cooling setup. More than 89% of the screening solutions were directly suitable for HPC. This achievement represents a drastic improvement for crystals that suffered from cryoprotection or were not previously eligible for cryoprotection.
[Mh] Termos MeSH primário: Cristalização
Cristalografia por Raios X/instrumentação
Síncrotrons
[Mh] Termos MeSH secundário: Animais
Galinhas
Temperatura Baixa
Concanavalina A/química
Criopreservação
Crioprotetores/química
Muramidase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cryoprotective Agents); 11028-71-0 (Concanavalin A); EC 3.2.1.- (hen egg lysozyme); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1107/S2059798317016357


  8 / 20325 MEDLINE  
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[PMID]:28740983
[Au] Autor:Consentius P; Gohlke U; Loll B; Alings C; Heinemann U; Wahl MC; Risse T
[Ad] Endereço:Freie Universität Berlin, Institute of Chemistry and Biochemistry, Takustr. 3, 14195 Berlin, Germany. risse@chemie.fu-berlin.de.
[Ti] Título:Combining EPR spectroscopy and X-ray crystallography to elucidate the structure and dynamics of conformationally constrained spin labels in T4 lysozyme single crystals.
[So] Source:Phys Chem Chem Phys;19(31):20723-20734, 2017 Aug 09.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Electron paramagnetic resonance (EPR) spectroscopy in combination with site-directed spin labeling is used to investigate the structure and dynamics of conformationally constrained spin labels in T4 lysozyme single crystals. Within a single crystal, the oriented ensemble of spin bearing moieties results in a strong angle dependence of the EPR spectra. A quantitative description of the EPR spectra requires the determination of the unit cell orientation with respect to the sample tube and the orientation of the spin bearing moieties within the crystal lattice. Angle dependent EPR spectra were analyzed by line shape simulations using the stochastic Liouville equation approach developed by Freed and co-workers and an effective Hamiltonian approach. The gain in spectral information obtained from the EPR spectra of single crystalline samples taken at different frequencies, namely the X-band and Q-band, allows us to discriminate between motional models describing the spectra of isotropic solutions similarly well. In addition, it is shown that the angle dependent single crystal spectra allow us to identify two spin label rotamers with very similar side chain dynamics. These results demonstrate the utility of single crystal EPR spectroscopy in combination with spectral line shape simulation techniques to extract valuable dynamic information not readily available from the analysis of isotropic systems. In addition, it will be shown that the loss of electron density in high resolution diffraction experiments at room temperature does not allow us to conclude that there is significant structural disorder in the system.
[Mh] Termos MeSH primário: Bacteriófago T4/enzimologia
Muramidase/química
Proteínas Virais/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Espectroscopia de Ressonância de Spin Eletrônica
Ligações de Hidrogênio
Estrutura Terciária de Proteína
Marcadores de Spin
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Spin Labels); 0 (Viral Proteins); EC 3.2.1.17 (Muramidase)
[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:170726
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp03144k


  9 / 20325 MEDLINE  
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[PMID]:28745873
[Au] Autor:Nauser T; Gebicki JM
[Ad] Endereço:Department of Chemistry and Applied Biosciences, Swiss Federal Institute of Technology , Zurich CH8093, Switzerland.
[Ti] Título:Physiological Concentrations of Ascorbate Cannot Prevent the Potentially Damaging Reactions of Protein Radicals in Humans.
[So] Source:Chem Res Toxicol;30(9):1702-1710, 2017 09 18.
[Is] ISSN:1520-5010
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The principal initial biological targets of free radicals formed under conditions of oxidative stress are the proteins. The most common products of the interaction are carbon-centered alkyl radicals which react rapidly with oxygen to form peroxyl radicals and hydroperoxides. All these species are reactive, capable of propagating the free radical damage to enzymes, nucleic acids, lipids, and endogenous antioxidants, leading finally to the pathologies associated with oxidative stress. The best chance of preventing this chain of damage is in early repair of the protein radicals by antioxidants. Estimate of the effectiveness of the physiologically significant antioxidants requires knowledge of the antioxidant tissue concentrations and rate constants of their reaction with protein radicals. Previous studies by pulse radiolysis have shown that only ascorbate can repair the Trp and Tyr protein radicals before they form peroxyl radicals under physiological concentrations of oxygen. We have now extended this work to other protein C-centered radicals generated by hydroxyl radicals because these and many other free radicals formed under oxidative stress can produce secondary radicals on virtually any amino acid residue. Pulse radiolysis identified two classes of rate constants for reactions of protein radicals with ascorbate, a faster one in the range (9-60) × 10 M s and a slow one with a range of (0.5-2) × 10 M s . These results show that ascorbate can prevent further reactions of protein radicals only in the few human tissues where its concentration exceeds about 2.5 mM.
[Mh] Termos MeSH primário: Ácido Ascórbico/química
Radicais Livres/química
Proteínas/química
[Mh] Termos MeSH secundário: Raios gama
Seres Humanos
Insulina/química
Muramidase/química
Óxidos de Nitrogênio/química
Radiólise de Impulso
Albumina Sérica/química
Espectrofotometria Ultravioleta
Triptofano/química
Tirosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Free Radicals); 0 (Insulin); 0 (Nitrogen Oxides); 0 (Proteins); 0 (Serum Albumin); 42HK56048U (Tyrosine); 8DUH1N11BX (Tryptophan); EC 3.2.1.17 (Muramidase); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180127
[Lr] Data última revisão:
180127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1021/acs.chemrestox.7b00160


  10 / 20325 MEDLINE  
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[PMID]:29244473
[Au] Autor:Rotkina AS; Pronina IV; Lazarev VN; Akhaev DN; Baskova IP
[Ti] Título:Destabilase-lysozyme-2 - original recombinant thrombolytic preparation of medicinal leech inhibits horse platelets aggregation.
[So] Source:Patol Fiziol Eksp Ter;60(3):47-51, 2016 Jul-Sep.
[Is] ISSN:0031-2991
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:The purpose. Identifying the capacity of the medicinal leech novel original recombinant thrombolytic preparation Destabilase-Lysozyme-2 to inhibit the blood platelet aggregation. Methods: Gene of destabilase-lysozyme. ds2 (mlDL-Ds2 ), was cloned in E.coli cells. Recombinant protein was isolated in denaturing conditions using metal-chelate chromatography followed by denaturation of the polypeptide by rapid dilution in exact accordance with the procedure described by Kurdyumov A.S. et al. ( 2016, Russian Journal of Bioorganic Chemistry, v.42, s. 42-52). Blood was collected from the jugular vein of 18 horses. The functional status of platelets in the presence of different destabilase-lysozyme concentrations were evaluated for their aggregation in Platelet Rich Plasma ( PRP) and in Washed Platelet suspension (WP) using aggregometers Chrono-Log-700 and Сhrono-Log-560, USA560, США. As used aggregation inducers of ADP, collagen type III and human thrombin. Results: First demonstrated the ability of newly synthesized (Kurdyumov A.S. et al. 2016, Russian Journal of Bioorganic Chemistry, v42, s. 42-52) thrombolytic recombinant enzyme destabilase-lyzosyme to inhibit more than 40% of ADP-stimulated PRP aggregation and ADP- stimulated aggregation of horse blood washed platelets. Conclusion: The ability of destabilase-lyzosyme -2 to inhibit platelets aggregation extends biological properties of recombinant thrombolytic enzyme, pre-clinical trials which resulted in the end of 2015.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Endopeptidases
Fibrinolíticos
Hirudo medicinalis/enzimologia
Muramidase
Agregação Plaquetária/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Endopeptidases/química
Endopeptidases/isolamento & purificação
Endopeptidases/farmacologia
Fibrinolíticos/química
Fibrinolíticos/isolamento & purificação
Fibrinolíticos/farmacologia
Cavalos
Muramidase/química
Muramidase/isolamento & purificação
Muramidase/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibrinolytic Agents); EC 3.2.1.17 (Muramidase); EC 3.4.- (Endopeptidases); EC 3.4.99.- (fibrin destabilase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE



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