Base de dados : MEDLINE
Pesquisa : D09.698.629.305.540 [Categoria DeCS]
Referências encontradas : 288 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 29 ir para página                         

  1 / 288 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28193904
[Au] Autor:Narang A; Oehler S
[Ad] Endereço:Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, Hauz Khas, New Delhi, India.
[Ti] Título:Effector Overlap between the and Operons of Escherichia coli: Induction of the Operon with ß-Galactosides.
[So] Source:J Bacteriol;199(9), 2017 May 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The (lactose) operon (which processes ß-galactosides) and the (melibiose) operon (which processes α-galactosides) of have a close historical connection. A number of shared substrates and effectors of the permeases and regulatory proteins have been reported over the years. Until now, ß-thiogalactosides like TMG (methyl-ß-d-thiogalactopyranoside) and IPTG (isopropyl-ß-d-thiogalactopyranoside) have not generally been considered to be inducers of the operon. The same is true for ß-galactosides such as lactose [ß-d-galactopyranosyl-(1→4)-d-glucose], which is a substrate but is not itself an inducer of the operon. This report shows that all three sugars can induce the operon significantly when they are accumulated in the cell by Lac permease. Strong induction by ß-thiogalactosides is observed in the presence of Lac permease, and strong induction by lactose (more than 200-fold) is observed in the absence of ß-galactosidase. This finding calls for reevaluation of TMG uptake experiments as assays for Lac permease that were performed with strains. The typical textbook picture of bacterial operons is that of stand-alone units of genetic information that perform, in a regulated manner, well-defined cellular functions. Less attention is given to the extensive interactions that can be found between operons. Well-described examples of such interactions are the effector molecules shared by the and operons. Here, we show that this set has to be extended to include ß-galactosides, which have been, until now, considered not to effect the expression of the operon. That they can be inducers of the operon as well as the operon has not been noted in decades of research because of the genetic background used in previous studies.
[Mh] Termos MeSH primário: Escherichia coli/genética
Óperon Lac
Melibiose/genética
Óperon
[Mh] Termos MeSH secundário: Galactosídeos/genética
Galactosídeos/farmacologia
Glucose/farmacologia
Lactose/farmacologia
Melibiose/metabolismo
Proteínas de Membrana Transportadoras
beta-Galactosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Galactosides); 0 (Membrane Transport Proteins); 0 (beta-galactoside); 9068-45-5 (lactose permease); 9B1VBE526I (Melibiose); EC 3.2.1.23 (beta-Galactosidase); IY9XDZ35W2 (Glucose); J2B2A4N98G (Lactose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE


  2 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27577255
[Au] Autor:Zhou Y; Zhu Y; Dai L; Men Y; Wu J; Zhang J; Sun Y
[Ad] Endereço:Key Laboratory for Industrial Fermentation Microbiology, Ministry of Education; College of Biotechnology, Tianjin University of Science & Technology, Tianjin, 300457, China.
[Ti] Título:Efficiency Analysis and Mechanism Insight of that Whole-Cell Biocatalytic Production of Melibiose from Raffinose with Saccharomyces cerevisiae.
[So] Source:Appl Biochem Biotechnol;181(1):407-423, 2017 Jan.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Melibiose is widely used as a functional carbohydrate. Whole-cell biocatalytic production of melibiose from raffinose could reduce its cost. However, characteristics of strains for whole-cell biocatalysis and mechanism of such process are unclear. We compared three different Saccharomyces cerevisiae strains (liquor, wine, and baker's yeasts) in terms of concentration variations of substrate (raffinose), target product (melibiose), and by-products (fructose and galactose) in whole-cell biocatalysis process. Distinct difference was observed in whole-cell catalytic efficiency among three strains. Furthermore, activities of key enzymes (invertase, α-galactosidase, and fructose transporter) involved in process and expression levels of their coding genes (suc2, mel1, and fsy1) were investigated. Conservation of key genes in S. cerevisiae strains was also evaluated. Results show that whole-cell catalytic efficiency of S. cerevisiae in the raffinose substrate was closely related to activity of key enzymes and expression of their coding genes. Finally, we summarized characteristics of producing strain that offered advantages, as well as contributions of key genes to excellent strains. Furthermore, we presented a dynamic mechanism model to achieve some mechanism insight for this whole-cell biocatalytic process. This pioneering study should contribute to improvement of whole-cell biocatalytic production of melibiose from raffinose.
[Mh] Termos MeSH primário: Biocatálise
Melibiose/biossíntese
Rafinose/química
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Frutose/biossíntese
Galactose/biossíntese
Melibiose/química
Proteínas de Membrana Transportadoras/química
Proteínas de Membrana Transportadoras/genética
Rafinose/metabolismo
Saccharomyces cerevisiae/enzimologia
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
beta-Frutofuranosidase/química
beta-Frutofuranosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Transport Proteins); 0 (Saccharomyces cerevisiae Proteins); 30237-26-4 (Fructose); 9B1VBE526I (Melibiose); EC 3.2.1.26 (SUC2 protein, S cerevisiae); EC 3.2.1.26 (beta-Fructofuranosidase); N5O3QU595M (Raffinose); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170126
[Lr] Data última revisão:
170126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160901
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2220-7


  3 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27794607
[Au] Autor:Tanaka S; Shinoki A; Hara H
[Ad] Endereço:Laboratory of Nutritional Biochemistry, Division of Applied Bioscience, Graduate School of agriculture, Hokkaido University , Sapporo, Hokkaido 060-8589, Japan.
[Ti] Título:Melibiose, a Nondigestible Disaccharide, Promotes Absorption of Quercetin Glycosides in Rat Small Intestine.
[So] Source:J Agric Food Chem;64(49):9335-9341, 2016 Dec 14.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We demonstrated that melibiose, a nondigestible disaccharide composed of galactose and glucose with α-1,6 glycoside linkage, promotes the absorption of water-soluble quercetin glycosides in ligated small intestinal loop of anesthetized rats. Water-soluble quercetin glycoside, a quercetin-3-O-glucoside mixture (Q3GM), includes quercetin-3-O-glucoside (Q3G, 31.9%), mono (21.2%) and di (17.1%), glucose adducts with α-1,4 linkages. After instillation of Q3GM into the intestinal loop with or without melibiose, the plasma concentration of quercetin derivatives in the portal blood was considerably higher in the melibiose group at 60 min. Furthermore, we evaluated the hydrolytic rate of Q3G by the mucosal homogenate of the small intestine with six different disaccharides. Melibiose and isomaltose, which have α-1,6 glycoside linkage, were found to promote Q3G hydrolysis to aglycone. These results suggest that melibiose promotes quercetin glycoside absorption in rats by increasing glycoside hydrolysis in the intestinal lumen and that α-1,6 linkage is involved in this process.
[Mh] Termos MeSH primário: Glicosídeos/metabolismo
Intestino Delgado/metabolismo
Melibiose/metabolismo
Quercetina/metabolismo
[Mh] Termos MeSH secundário: Animais
Absorção Intestinal
Masculino
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycosides); 9B1VBE526I (Melibiose); 9IKM0I5T1E (Quercetin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE


  4 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27321131
[Au] Autor:Lipiäinen T; Peltoniemi M; Räikkönen H; Juppo A
[Ad] Endereço:Division of Pharmaceutical Chemistry and Technology, Faculty of Pharmacy, Formulation and Industrial Pharmacy Unit, Viikinkaari 5E, P.O. Box 56, FI-00014, University of Helsinki, Finland. Electronic address: tiina.lipiainen@helsinki.fi.
[Ti] Título:Spray-dried amorphous isomalt and melibiose, two potential protein-stabilizing excipients.
[So] Source:Int J Pharm;510(1):311-22, 2016 Aug 20.
[Is] ISSN:1873-3476
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The possibility of producing amorphous isomalt and melibiose by spray drying was studied. The impact of process parameters on yield and solid-state stability was compared to sucrose and trehalose. All powders remained amorphous during 2-3 weeks. Processing was challenging due to powder stickiness. Low-temperature and low-humidity drying processes generally performed best. Most isomalt and sucrose powder was retrieved when using 60°C inlet temperature, 800L/h atomizing rate, 1.4ml/min feed rate, 15% concentration and 100% aspirator rate, giving 42-43°C outlet temperature. Isomalt was the most problematic, because it had the lowest Tg and became sticky very easily, therefore process parameters needed to be precisely balanced. There was more freedom in designing processes for melibiose but best yields were obtained with low-temperature (50°C inlet temperature, 800L/h atomizing rate, 4.9ml/min feed rate, 10% concentration and 100% aspirator, 39°C outlet temperature). Trehalose was different in that higher temperatures resulted in better yields. Yet, trehalose generally contained the highest moisture contents. The possibility to produce amorphous isomalt and melibiose at low-temperature process conditions makes them promising considering spray drying applications for heat-sensitive proteins. Melibiose is a better candidate than isomalt because of easier processability and superior solid-state stability.
[Mh] Termos MeSH primário: Dissacarídeos/química
Excipientes/química
Melibiose/química
Estabilidade Proteica
Álcoois Açúcares/química
[Mh] Termos MeSH secundário: Dissacarídeos/farmacologia
Composição de Medicamentos
Excipientes/farmacologia
Melibiose/farmacologia
Tamanho da Partícula
Estabilidade Proteica/efeitos dos fármacos
Álcoois Açúcares/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disaccharides); 0 (Excipients); 0 (Sugar Alcohols); 64519-82-0 (Palatinit); 9B1VBE526I (Melibiose)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170419
[Lr] Data última revisão:
170419
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160621
[St] Status:MEDLINE


  5 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27254139
[Au] Autor:Sakaki Y; Tashiro M; Katou M; Sakuma C; Hirano T; Hakamata W; Nishio T
[Ad] Endereço:a Department of Chemistry and Life Science, College of Bioresource Sciences , Nihon University , Fujisawa , Japan.
[Ti] Título:Enzymatic synthesis of novel oligosaccharides from N-acetylsucrosamine and melibiose using Aspergillus niger α-galactosidase, and properties of the products.
[So] Source:Biosci Biotechnol Biochem;80(9):1836-42, 2016 Sep.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Two kinds of oligosaccharides, N-acetylraffinosamine (RafNAc) and N-acetylplanteosamine (PlaNAc), were synthesized from N-acetylsucrosamine and melibiose using the transgalactosylation activity of Aspergillus niger α-galactosidase. RafNAc and PlaNAc are novel trisaccharides in which d-glucopyranose residues in raffinose (Raf) and planteose are replaced with N-acetyl-d-glucosamine. These trisaccharides were more stable in acidic solution than Raf. RafNAc was hydrolyzed more rapidly than Raf by α-galactosidase of green coffee bean. In contrast, RafNAc was not hydrolyzed by Saccharomyces cerevisiae invertase, although Raf was hydrolyzed well by this enzyme. These results indicate that the physicochemical properties and steric structure of RafNAc differ considerably from those of Raf.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Oligossacarídeos/biossíntese
alfa-Galactosidase/metabolismo
[Mh] Termos MeSH secundário: Hidrólise
Melibiose/química
Oligossacarídeos/química
Rafinose/biossíntese
Rafinose/química
Saccharomyces cerevisiae
alfa-Galactosidase/genética
beta-Frutofuranosidase/genética
beta-Frutofuranosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (N-acetylsucrosamine); 0 (Oligosaccharides); 9B1VBE526I (Melibiose); EC 3.2.1.22 (alpha-Galactosidase); EC 3.2.1.26 (beta-Fructofuranosidase); N5O3QU595M (Raffinose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160603
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2016.1189316


  6 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27020280
[Au] Autor:Gong W; Xu L; Gu G; Lu L; Xiao M
[Ad] Endereço:State Key Lab of Microbial Technology, National Glycoengineering Research Center, Shandong Provincial Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, 250100, People's Republic of China.
[Ti] Título:Efficient and regioselective synthesis of globotriose by a novel α-galactosidase from Bacteroides fragilis.
[So] Source:Appl Microbiol Biotechnol;100(15):6693-702, 2016 Aug.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Globotriose (Galα1-4Galß1-4Glc) is an important cell surface epitope that acts as the receptor for Shiga-like toxins, and it is also the core structure of Globo H and SSEA4 that are tumor-associated glycans. Hence, the enzymatic synthesis of globotriose would be necessary for the development of carbohydrate-based therapeutics for bacterial infections and cancers. Here, a novel GH27 α-galactosidase gene (agaBf3S), a 1521-bp DNA encoding 506 amino acids with a calculated molecular mass of 57.7 kDa, from Bacteroides fragilis NCTC9343 was cloned and heterogeneously expressed in Escherichia coli. The recombinant enzyme AgaBf3S preferentially hydrolyzed p-nitrophenyl-α-D-galactopyranoside (pNPαGal) in all tested nitrophenyl glycosides. It showed maximum activity at pH 4.5 and 40 °C, and it was stable at pH 4.0-11.0 below 40 °C and metal-independent. The K m and k cat values for pNPαGal, melibiose, and globotriose were 1.27 mM and 172.97 S(-1), 62.76 mM and 17.74 S(-1), and 4.62 mM and 388.45 S(-1), respectively. AgaBf3S could transfer galactosyl residue from pNPαGal to lactose (Galß1-4Glc) with high efficiency and strict α1-4 regioselectivity. The effects of initial substrate concentration, pH, temperature, and reaction time on transglycosylation reaction catalyzed by AgaBf3S were studied in detail. AgaBf3S could synthesize globotriose as a single transglycosylation product with a maximum yield of 32.4 % from 20 mM pNPαGal and 500 mM lactose (pH 4.5) at 40 °C for 30 min. This new one-enzyme one-step synthetic reaction is simple, fast, and low cost, which provides a promising alternative to the current synthetic methods for access to pharmaceutically important Galα1-4-linked oligosaccharides.
[Mh] Termos MeSH primário: Bacteroides fragilis/enzimologia
Escherichia coli/metabolismo
Nitrofenilgalactosídeos/metabolismo
Trissacarídeos/biossíntese
alfa-Galactosidase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bacteroides fragilis/genética
Escherichia coli/genética
Melibiose/biossíntese
Alinhamento de Sequência
Especificidade por Substrato
alfa-Galactosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Trisaccharides); 28347-45-7 (Nitrophenylgalactosides); 3150-24-1 (4-nitrophenylgalactoside); 66580-68-5 (globotriose); 9B1VBE526I (Melibiose); EC 3.2.1.22 (alpha-Galactosidase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170202
[Lr] Data última revisão:
170202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160330
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7464-1


  7 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26940051
[Au] Autor:Díez-Municio M; Herrero M; de Las Rivas B; Muñoz R; Jimeno ML; Moreno FJ
[Ad] Endereço:Instituto de Investigación en Ciencias de la Alimentación, CIAL (CSIC-UAM), CEI (UAM+CSIC), C/ Nicolás Cabrera 9, 28049, Madrid, Spain.
[Ti] Título:Synthesis and structural characterization of raffinosyl-oligofructosides upon transfructosylation by Lactobacillus gasseri DSM 20604 inulosucrase.
[So] Source:Appl Microbiol Biotechnol;100(14):6251-63, 2016 Jul.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A new process based on enzymatic synthesis of a series of raffinose-derived oligosaccharides or raffinosyl-oligofructosides (RFOS) with degree of polymerization (DP) from 4 to 8 was developed in the presence of raffinose. This process involves a transfructosylation reaction catalyzed by an inulosucrase from Lactobacillus gasseri DSM 20604 (IS). The main synthesized RFOS were structurally characterized by nuclear magnetic resonance (NMR). According to the elucidated structures, RFOS consist of ß-2,1-linked fructose unit(s) to raffinose: α-D-galactopyranosyl-(1 → 6)-α-D-glucopyranosyl-(1↔2)-ß-D-fructofuranosyl-((1 ← 2)-ß-D-fructofuranoside)n (where n refers to the number of transferred fructose moieties). The maximum yield of RFOS was 33.4 % (in weight respect to the initial amount of raffinose) and was obtained at the time interval of 8-24 h of transfructosylation reaction initiated with 50 % (w/v) of raffinose. Results revealed the high acceptor and donor affinity of IS towards raffinose, being fairly comparable with that of sucrose for the production of fructooligosaccharides (FOS), including when both carbohydrates coexisted (sucrose/raffinose mixture, 250 g L(-1) each). The production of RFOS was also attempted in the presence of sucrose/melibiose mixtures; in this case, the predominant acceptor-product formed was raffinose followed by a minor production of a series of oligosaccharides with varying DP. The easiness of RFOS synthesis and the structural similarities with both raffinose and fructan series of oligosaccharides warrant the further study of the potential bioactive properties of these unexplored oligosaccharides.
[Mh] Termos MeSH primário: Hexosiltransferases/metabolismo
Lactobacillus gasseri/enzimologia
Rafinose/química
[Mh] Termos MeSH secundário: Meios de Cultura/química
Frutanos/química
Frutose/química
Microbiologia Industrial
Imagem por Ressonância Magnética
Melibiose/química
Proteínas Recombinantes/metabolismo
Sacarose/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Fructans); 0 (Recombinant Proteins); 30237-26-4 (Fructose); 57-50-1 (Sucrose); 9B1VBE526I (Melibiose); EC 2.4.1.- (Hexosyltransferases); EC 2.4.1.9 (inulosucrase); N5O3QU595M (Raffinose)
[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:160305
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7405-z


  8 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26786171
[Au] Autor:Gao DM; Kobayashi T; Adachi S
[Ad] Endereço:a Division of Food Science and Biotechnology , Graduate School of Agriculture, Kyoto University , Kyoto , Japan.
[Ti] Título:Production of keto-disaccharides from aldo-disaccharides in subcritical aqueous ethanol.
[So] Source:Biosci Biotechnol Biochem;80(5):998-1005, 2016 May.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Isomerization of disaccharides (maltose, isomaltose, cellobiose, lactose, melibiose, palatinose, sucrose, and trehalose) was investigated in subcritical aqueous ethanol. A marked increase in the isomerization of aldo-disaccharides to keto-disaccharides was noted and their hydrolytic reactions were suppressed with increasing ethanol concentration. Under any study condition, the maximum yield of keto-disaccharides produced from aldo-disaccharides linked by ß-glycosidic bond was higher than that produced from aldo-disaccharides linked by α-glycosidic bond. Palatinose, a keto-disaccharide, mainly underwent decomposition rather than isomerization in subcritical water and subcritical aqueous ethanol. No isomerization was noted for the non-reducing disaccharides trehalose and sucrose. The rate constant of maltose to maltulose isomerization almost doubled by changing solvent from subcritical water to 80 wt% aqueous ethanol at 220 °C. Increased maltose monohydrate concentration in feed decreased the conversion of maltose and the maximum yield of maltulose, but increased the productivity of maltulose. The maximum productivity of maltulose was ca. 41 g/(h kg-solution).
[Mh] Termos MeSH primário: Dissacarídeos/química
Etanol/química
Água/química
[Mh] Termos MeSH secundário: Celobiose/química
Hidrólise
Isomaltose/análogos & derivados
Isomaltose/química
Cinética
Lactose/química
Espectroscopia de Ressonância Magnética
Maltose/química
Melibiose/química
Soluções
Estereoisomerismo
Sacarose/química
Trealose/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disaccharides); 0 (Solutions); 059QF0KO0R (Water); 16462-44-5 (Cellobiose); 3K9958V90M (Ethanol); 57-50-1 (Sucrose); 67I334IX2M (Isomaltose); 69-79-4 (Maltose); 9B1VBE526I (Melibiose); B8WCK70T7I (Trehalose); J2B2A4N98G (Lactose); V59P50X4UY (isomaltulose)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170123
[Lr] Data última revisão:
170123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160121
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2015.1127135


  9 / 288 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:26295831
[Au] Autor:Lin CH; Wu YR; Yang JM; Chen WL; Chao CY; Chen IC; Lin TH; Wu YC; Hsu KC; Chen CM; Lee GC; Hsieh-Li HM; Lee CM; Lee-Chen GJ
[Ti] Título:Novel Lactulose and Melibiose Targeting Autophagy to Reduce PolyQ Aggregation in Cell Models of Spinocerebellar Ataxia 3.
[So] Source:CNS Neurol Disord Drug Targets;15(3):351-9, 2016.
[Is] ISSN:1996-3181
[Cp] País de publicação:United Arab Emirates
[La] Idioma:eng
[Ab] Resumo:Trehalose, a chemical chaperone and mTOR-independent autophagy enhancer, has shown promise in models of Huntington's disease, Parkinson's disease and tauopathies. In this study, two trehalase analogs, lactulose and melibiose, were examined for their potentials in spinocerebellar ataxia treatment. Using a SCA3 ATXN3/Q75-GFP cell model, we found that the ATXN3/Q75 aggregation was significantly prohibited by lactulose and melibiose because of their abilities to up-regulate autophagy. Meanwhile, lactulose and melibiose reduced reactive oxygen species production in ATXN3/Q75 cells. Both of them further inhibited the ATXN3/Q75 aggregation in neuronally differentiated SH-SY5Y cells. These findings suggest the therapeutic applications of novel trehalose analogs in polyglutamine aggregation-associated neurodegenerative diseases.
[Mh] Termos MeSH primário: Ataxina-3/metabolismo
Autofagia/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Lactulose/farmacologia
Melibiose/farmacologia
Peptídeos/metabolismo
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Análise de Variância
Ataxina-3/genética
Autofagia/genética
Linhagem Celular Tumoral
Regulação da Expressão Gênica/genética
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Seres Humanos
Lactulose/química
Melibiose/química
Neuroblastoma/patologia
Peptídeos/genética
Agregação Patológica de Proteínas/tratamento farmacológico
Espécies Reativas de Oxigênio/metabolismo
Proteínas Repressoras/genética
Transfecção
Trealose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 0 (Reactive Oxygen Species); 0 (Repressor Proteins); 147336-22-9 (Green Fluorescent Proteins); 26700-71-0 (polyglutamine); 4618-18-2 (Lactulose); 9B1VBE526I (Melibiose); B8WCK70T7I (Trehalose); EC 3.4.19.12 (ATXN3 protein, human); EC 3.4.19.12 (Ataxin-3)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150822
[St] Status:MEDLINE


  10 / 288 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
[PMID]:26547958
[Au] Autor:Borzova NV; Varbanets LD
[Ti] Título:STABILITY OF NATIVE AND MODIFIED α-GALACTOSIDASE OF Cladosporium cladosporioides.
[So] Source:Ukr Biochem J;87(4):5-12, 2015 Jul-Aug.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:By modifying carbohydrate component of glycoproteins it is possible to elucidate its role in manifestation of structural and functional properties of the enzyme. The comparison of activity and stability of the native and modified by oxidation with sodium periodate α-galactosidase of Cladosporium cladosporioides was carried out. To determine α-galactosidase activity the authors used n-nitrophenyl synthetic substrate, as well as melibiose; raffinose and stachyose. Modification of the carbohydrate component had a significant effect on catalytic properties of the enzyme. Both the reduction of V and enzyme affinity for natural and synthetic substrates were observed The native enzyme retained more than 50% ofthe maximum activity in the range of 20-60 °C, while for the modified enzyme under the same conditions that temperature range was 30-50 °C. The modified α-galactosidase demonstrated a higher thermal stability under neutral pH conditions. The residual activity of the modified α-galactosidase was about 30% when treated with 70% (v/v) methanol, ethanol and propanol. About 50% of initial activity was observed when 40% ethanol and propanol, and 50% methanol were used. It was shown that the modification of C. cladosporioides α-galactosidase by sodium periodate is accompanied by a significant decrease in enzyme activity and stability, probably caused by topological changes in the tertiary and quaternary structure of the protein molecule.
[Mh] Termos MeSH primário: Cladosporium/química
Proteínas Fúngicas/química
alfa-Galactosidase/química
[Mh] Termos MeSH secundário: Cladosporium/enzimologia
Ensaios Enzimáticos
Estabilidade Enzimática
Proteínas Fúngicas/isolamento & purificação
Concentração de Íons de Hidrogênio
Cinética
Melibiose/química
Oligossacarídeos/química
Oxidantes/química
Oxirredução
Ácido Periódico/química
Conformação Proteica
Rafinose/química
Relação Estrutura-Atividade
Especificidade por Substrato
Temperatura Ambiente
alfa-Galactosidase/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Oligosaccharides); 0 (Oxidants); 10450-60-9 (Periodic Acid); 25VX64653N (stachyose); 9B1VBE526I (Melibiose); B45A1BUM4Q (metaperiodate); EC 3.2.1.22 (alpha-Galactosidase); N5O3QU595M (Raffinose)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:151109
[Lr] Data última revisão:
151109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151110
[St] Status:MEDLINE



página 1 de 29 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde