Search results for "recombinant"

showing 10 items of 1150 documents

The redox state regulates RNA degradation in the chloroplast of Chlamydomonas reinhardtii.

1999

Abstract A Chlamydomonas reinhardtii chloroplast transformant, designated MU7, carrying a chimeric (rbcL promoter: β-glucuronidase [GUS]:psaB 3′ end) gene whose transcripts have been found previously to be unstable in light (half-life of 20 min in light as opposed to a half-life of 5 h in the dark), was used to study the role of electron transport and of the redox state in the degradation of chloroplast transcripts in the light. Blocking photosynthetic electron transport with 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) prevented the light-dependent breakdown of the pool of GUS transcripts in MU7 cells. Diamide, an oxidizing agent, caused a measurable delay in the degradation of GUS trans…

ChloroplastsLightTranscription GeneticPhysiologyCell SurvivalRecombinant Fusion ProteinsMolecular Sequence DataChlorophyceaeChlamydomonas reinhardtiiPlant SciencePolymerase Chain ReactionDithiothreitolCell Linechemistry.chemical_compoundTranscription (biology)Gene Expression Regulation PlantGeneticsAnimalsDNA PrimersGlucuronidasebiologyBase SequencefungiRNAfood and beveragesDCMUbiology.organism_classificationElectron transport chainCell biologyChloroplastDithiothreitolBiochemistrychemistryRNA PlantDiuronOxidation-ReductionChlamydomonas reinhardtiiResearch ArticlePlant physiology
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Sample streaks and smears in immobilized pH gradient gels

1996

In immobilized pH gradient (IPG) gel formulations as wide as pH 4-9, encompassing neutrality and containing the pK 7.0 acrylamido buffer as one of the buffering ions, smears are directly proportional to the total amount of the pK 7.0 species. At a total level of 10 mM pK 7.0 in these gel formulations, severe smears occur not only for mildly hydrophobic proteins (e.g., recombinant alcalase and termamylase) but also for the relatively hydrophilic pI marker proteins. Streaks and smears are essentially abolished in recipes devoid of the pK 7.0 compound or in formulations containing a maximum of 3 mM of this component. Although partitioning in water/n-octanol has shown the pK 7.0 acrylamido buff…

ChromatographyChemistryIsoelectric focusingClinical BiochemistryHydrogen-Ion ConcentrationBiochemistryAnalytical Chemistrylaw.inventionHydrophobic effectlawRecombinant DNASubtilisinsImmobilized pH gradientIsoelectric FocusingGelsElectrophoresis
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Insect immunity. Constitutive expression of a cysteine-rich antifungal and a linear antibacterial peptide in a termite insect

2001

0021-9258 (Print) Journal Article Research Support, Non-U.S. Gov't; Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively p…

ChromatographyCysteine/*chemistryIsoptera/*immunologyBase SequenceProtein ConformationfungiAntifungal Agents/*chemistry/isolation & purification/pharmacologyMolecular Sequence DataSequence HomologyImmunohistochemistryAmino AcidAnti-Bacterial Agents/*chemistry/isolation & purification/pharmacologyRecombinant Proteins/chemistry/isolation & purification/pharmacologyHigh Pressure LiquidAnimalsAmino Acid SequencePeptidesDNA Primers
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Study of conformational effects of recombinant interferon gamma adsorbed on a non-porous reversed-phase silica support.

1995

Abstract Reversed-phase chromatography is a powerful method for separating recombinant interferon γ and one of its analogues differing only by a single amino acid residue. Structural differences of the proteins explain this separation ability as demonstrated from adsorption studies on a non-porous reversed-phase support. To reveal the structural differences occurring in the adsorbed state, two different and independent methods were employed. The variation of the retention with the slope of the linear gradient gave information about the molecular contact area of the protein with the support. For different experimental conditions, these data were correlated with the adsorbent capacities measu…

ChromatographyRecombinant interferonChemistryProtein ConformationTemperatureGeneral ChemistrySilicon DioxideRecombinant Proteinslaw.inventionResidue (chemistry)Interferon-gammaAdsorptionlawPhase (matter)Recombinant DNAmedicineHumansInterferon gammaAdsorptionContact areaPorosityChromatography High Pressure Liquidmedicine.drugJournal of chromatography. B, Biomedical applications
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Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of α-actinin

2009

Abstract Background The PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, α-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown. Results In this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107–273) was largely unfolded in solution, but was able to interact with the α-actinin rod domain in vitro, and to co-localize with α-actinin on stress fibres in vivo. NMR analysis revealed that the ti…

Circular dichroismPDZ domaineducationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingActininmacromolecular substancesBiology03 medical and health sciences0302 clinical medicineCell Line TumorHumansActininAmino Acid Sequencelcsh:QH573-671Peptide sequenceActin030304 developmental biologyLIM domainFluorescent Dyes0303 health scienceslcsh:CytologyMicrofilament ProteinsCell BiologyLIM Domain ProteinsSurface Plasmon Resonancemusculoskeletal systemRecombinant ProteinsCell biologyProtein Structure TertiaryLHX3Peptides030217 neurology & neurosurgeryResearch ArticleProtein BindingBMC Cell Biology
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Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the V1VO ATPase from Aedes albopictus.

2007

The Asian tiger mosquito, Aedes albopictus, is commonly infected by the gregarine parasite Ascogregarina taiwanensis, which develops extracellularly in the midgut of infected larvae. The intracellular trophozoites are usually confined within a parasitophorous vacuole, whose acidification is generated and controlled by the V(1)V(O) ATPase. This proton pump is driven by ATP hydrolysis, catalyzed inside the major subunit A. The subunit A encoding gene of the Aedes albopictus V(1)V(O) ATPase was cloned in pET9d1-His(3) and the recombinant protein, expressed in the Escherichia coli Rosetta 2 (DE3) strain, purified by immobilized metal affinity- and ion-exchange chromatography. The purified prote…

Circular dichroismVacuolar Proton-Translocating ATPasesATPaseProtein subunitGene ExpressionGenes InsectBiologyIn Vitro Techniquesmedicine.disease_causelaw.inventionAdenosine TriphosphateATP hydrolysislawAedesCatalytic DomainmedicineAnimalsNucleotideCloning MolecularEscherichia coliDNA Primerschemistry.chemical_classificationPhotoaffinity labelingBase SequenceMolecular biologyProtein SubunitsSpectrometry FluorescenceBiochemistrychemistrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinRecombinant DNAInsect ProteinsBiotechnologyProtein expression and purification
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Strategies for improving production and purification of a recombinant protein: rP30 of Toxoplasma gondii expressed in the yeast Schizosaccharomyces p…

2007

Abstract Many problems concerned with the production and the purification of recombinant proteins must be addressed prior to launching an industrial production process. Among these problems, attention is focused on low-level expression that complicates the purification step and can jeopardise the process. The expression of a membrane protein, rP30, of Toxoplasma gondii in the yeast Schizosaccharomyces pombe led to a secretion of only 0.5 μg ml−1. In order to obtain a sufficient quantity for biochemical characterization and evaluation in vitro diagnostic test development, strategies for both production and purification had to be optimized. First, the influence of four nitrogen sources (three…

Clinical BiochemistryIon chromatographyProtozoan ProteinsAntigens ProtozoanRaw materialBiochemistryChromatography AffinityAnalytical Chemistrylaw.inventionAffinity chromatographylawSchizosaccharomycesYeast extractAnimalsBiomassChromatographybiologyChemistryCell BiologyGeneral Medicinebiology.organism_classificationYeastRecombinant ProteinsBiochemistrySchizosaccharomyces pombeFermentationRecombinant DNAFermentationToxoplasmaJournal of chromatography. B, Analytical technologies in the biomedical and life sciences
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Novel biosensor-based analytic device for the detection of anti-double-stranded DNA antibodies.

2007

AbstractBackground: Patients with systemic lupus erythematosus (SLE) develop a wide variety of serologic manifestations, including double-stranded DNA autoantibodies (anti-dsDNA). The determination of the potentially pathogenic autoantibodies is diagnostically relevant.Methods: We developed a novel surface plasmon resonance (SPR) biosensor chip for studies of dsDNA and anti-dsDNA binding. A synthetic oligonucleotide was coupled to biotinylated human transferrin, hybridized with the complementary antistrand, and ligated with a human recombinant dsDNA fragment 233 bp in length. After surface immobilization of this antigenic construct, diluted sera from SLE patients and healthy donors were ana…

Clinical BiochemistryPilot ProjectsBiosensing TechniquesBiologySensitivity and Specificitylaw.inventionchemistry.chemical_compoundAntigenimmune system diseaseslawHumansLupus Erythematosus SystemicSurface plasmon resonanceskin and connective tissue diseasesOligonucleotideBiochemistry (medical)DNASurface Plasmon ResonanceMolecular biologyReceptor–ligand kineticschemistryBiotinylationAntibodies AntinuclearRecombinant DNABiosensorDNAClinical chemistry
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Identification of Tumor-Associated Autoantigens With SEREX

2004

Serological analysis of tumor antigens by recombinant cDNA expression cloning (SEREX) allows the systematic cloning of tumor antigens recognized by the spontaneous autoantibody repertoire of cancer patients. For SEREX, cDNA expression libraries are constructed from fresh tumor specimens, packaged into lambda-phage vectors, and expressed recombinantly in Escherichia coli. Recombinant proteins expressed during the lytic infection of bacteria are transferred onto nitrocellulose membranes to be probed with diluted autologous patient serum for identification of clones reactive with high-titered IgG antibodies. This chapter describes the SEREX technology in detail.

CloningbiologyAntigenLytic cyclelawbiology.proteinAutoantibodyRecombinant DNAGenomic libraryAntibodyMolecular biologySerologylaw.invention
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Cloning and Characterization of Overlapping DNA Fragments of the Toxin A Gene of Clostridium difficile

1989

Clostridium difficile, a human pathogen, produces two very large protein toxins, A and B (250-600 kDa), which resist dissociation into subunits. To clone the toxin A gene, a genomic library of 3-8 kb chromosomal DNA fragments of C. difficile strain VPI 10463 established in pUC12 was screened with a rabbit polyclonal toxin A antiserum. Thirty-five clones were isolated which carried 2.5-7.0 kb inserts representing a 10 kb region of the C. difficile genome. All the inserts were oriented in the same direction, suggesting that toxin A gene expression was under control of the lac promoter of the pUC12 vector. Western blot experiments revealed the presence of low amounts of fusion proteins of vari…

ClostridiumDNA BacterialRecombinant Fusion ProteinsBacterial ToxinsBlotting WesternRestriction MappingClostridium difficile toxin ABiologyMolecular cloningmedicine.disease_causeMicrobiologyMolecular biologyMicrobiologyGene productEnterotoxinsPlasmidSubcloningGenes BacterialmedicineGenomic libraryCloning MolecularGeneEscherichia coliMicrobiology
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