Gfpuv
Mostrando 1-12 de 16 artigos, teses e dissertações.
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1. Remoção de endotoxina presente em meio fermentado contendo biomoléculas utilizando sistemas micelares de duas fases aquosas / Endotoxin removal from fermentation broth containing biomolecules using two-phase micellar system
Foi investigada a utilização de Sistema Micelar de Duas Fases Aquosas (SMDFA) para remoção de lipolissacarídeos (LPS) de preparações contendo proteínas recombinantes de interesse farmacêutico, como a proteína verde fluorescente (GFPuv). Os SMDFA são constituídos por soluções de tensoativos contendo micelas e oferecem ambientes hidrofóbico e hi
Publicado em: 2010
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2. Determinação dos parâmetros cinéticos de resistência térmica da Proteína Verde Fluorescente recombinante (GFPuv) / Determination of kinetic parameters of thermal resistance of the Green Fluorescent Protein (GFPuv)
Células transformadas de E.coli DH5-α expressando a proteína verde fluorescente (GFPuv, pico de excitação e emissão de 394nm e 509nm) foram submetidas a extração pelo método de partição de três fases (TPP) e o extrato obtido purificado por cromatografia de interação hidrofóbica (HIC). O objetivo principal deste trabalho foi estudar a termo
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 29/04/2003
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3. Extração, purificação e caracterização físico-química da proteína verde fluorescente recombinante (GFPuv) expressa em Escherichia coli
O aumento do uso da proteína verde fluorescente (GFPuv) como ferramenta de pesquisas biotecnológicas requer um estudo mais cuidadoso das propriedades bioquímicas e físicas da molécula de GFPuv. Este trabalho teve como objetivo a aplicação de métodos físicos e químicos para o isolamento, a extração da GFPuv de células de Escherichia coli DH5-±,
Revista Brasileira de Ciências Farmacêuticas. Publicado em: 2003-12
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4. Comparison between physical and chemical methods for permeation and extraction of green fluorescent protein (GFPuv) from Escherichia coliDH5-alpha / Comparação entre os métodos físico e químico de permeação e de extração da proteína verde fluorescente (GFPuv) de culturas de Escherichia coli dh5-alpha
A proteína verde fluorescente (GFPuv), pelo fato de ter como característica a emissão de luz verde fluorescente brilhante quando exposta à luz ultravioleta, tem sido utilizada como marcador em diversos campos de pesquisa. Células transformadas de Escherichia coli DH5-a expressando a GFPuv foram submetidas aos tratamentos: (i) permeação seletiva (conge
Publicado em: 2002
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5. Green Fluorescent Protein as a Marker in Rickettsia typhi Transformation
Transformation of rickettsiae is a recent accomplishment, but utility of this technique is limited due to the paucity of selectable markers suitable for use in this intracellular pathogen. We chose a green fluorescent protein variant optimized for fluorescence under UV lights (GFPUV) as a fluorometric marker and transformed Rickettsia typhi with an rpoB-GFPU
American Society for Microbiology.
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6. Selective Activation of sar Promoters with the Use of Green Fluorescent Protein Transcriptional Fusions as the Detection System in the Rabbit Endocarditis Model
The global regulatory locus sar is composed of three overlapping transcripts initiated from a triple-promoter system (designated P1, P3, and P2). To explore if the individual sar promoters are differentially expressed in vitro and in vivo, we constructed a shuttle plasmid (pALC1434) containing a promoterless gfpUV gene (a gfp derivative [Clontech]) preceded
American Society for Microbiology.
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7. Dual Labeling with Green Fluorescent Proteins for Confocal Microscopy
We report a dual labeling technique involving two green fluorescent protein (GFP) variants that is compatible with confocal microscopy. Two lasers were used to obtain images of (i) mixed cultures of cells, where one species contained GFPuv and another species contained GFPmut2 or GFPmut3, and (ii) a single species containing both GFPuv and GFPmut2 in the sam
American Society for Microbiology.
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8. Selective Permeation and Organic Extraction of Recombinant Green Fluorescent Protein (gfpuv) from Escherichia coli
BioMed Central.
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9. Green Fluorescent Protein as a Noninvasive Stress Probe in Resting Escherichia coli Cells
We constructed and characterized three stress probe plasmids which utilize a green fluorescent protein as a noninvasive reporter in order to elucidate Escherichia coli cellular stress responses in quiescent or resting cells. Cellular stress levels were easily detected by fusing three heat shock stress protein promoter elements, those of the heat shock transc
American Society for Microbiology.
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10. Optimization of Plasmid Maintenance in the Attenuated Live Vector Vaccine Strain Salmonella typhi CVD 908-htrA†
The broad objective of the research presented here is to develop a noncatalytic plasmid maintenance system for the stabilization of multicopy expression plasmids encoding foreign antigens in a Salmonella typhi live-vector vaccine strain such as CVD 908-htrA. We have enhanced the maintenance of expression plasmids at two independent levels. First, we removed
American Society for Microbiology.
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11. Characterization of the groESL Operon in Listeria monocytogenes: Utilization of Two Reporter Systems (gfp and hly) for Evaluating In Vivo Expression
The ability of intracellular pathogens to sense and adapt to the hostile environment of the host is an important factor governing virulence. We have sequenced the operon encoding the major heat shock proteins GroES and GroEL in the gram-positive food-borne pathogen Listeria monocytogenes. The operon has a conserved orientation in the order groES groEL. Upstr
American Society for Microbiology.
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12. Identification and Molecular Analysis of the Gene Encoding Rickettsia typhi Hemolysin
Rickettsia typhi, the causative agent of murine typhus, grows directly within the host cell cytoplasm, accumulating a large number of progeny, and eventually lyses the cells. Typhus group rickettsiae (R. typhi and R. prowazekii) adhere to and lyse human and sheep erythrocytes. However, the molecular mechanism underlying erythrocyte lysis by R. typhi has not
American Society for Microbiology.