Search results for "Poly(acrylamide)"

showing 10 items of 377 documents

Construction of an agglutination tool: recombinant Fab fragments biotinylated in vitro.

2009

The pComb3H vector system is used for constructing and panning recombinant antibody libraries. It allows for expression of monovalent Fab fragments, either on the surface of M13 phage, or in the form of soluble proteins secreted into the periplasmic space of bacteria. We constructed a modified pComb3H vector containing cDNA encoding for a 23-amino acid fragment of the Escherichia coli biotin carboxy carrier protein (BCCP), which is an acceptor sequence for biotinylation. The vector was used to express the Fab fragment recognizing human glycophorin A. The purified Fab fragment containing this biotin acceptor sequence was effectively biotinylated in vitro using biotin ligase (BirA). The speci…

ErythrocytesBlotting WesternBioengineeringlaw.inventionchemistry.chemical_compoundImmunoglobulin Fab FragmentsBiotinlawAgglutination TestsGlycophorinHumansBiotinylationGlycophorinsMolecular BiologybiologyChemistryHemagglutinationGeneral MedicinePeriplasmic spaceAvidinMolecular biologyPrimary and secondary antibodiesRecombinant ProteinsAgglutination (biology)BiochemistryBiotinylationbiology.proteinRecombinant DNAChromatography GelElectrophoresis Polyacrylamide GelBiotechnologyAvidinProtein BindingNew biotechnology
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Mobility of Acetylated Histones in Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis

1999

Abstract We describe an altered mobility for acetylated histone isoforms in sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Isoforms of histones H3 and H4 with a higher acetylation degree have a slightly faster electrophoretic mobility. Since acetylation neutralizes the positive charge of the e-amino group of lysine, without significantly changing the molecular mass of the protein, the acetylation-dependent mobility shift could be explained by the increase of the net negative charge of the SDS–histone complexes. A possible consequence of this differential mobility for the acetylation site determination by protein microsequencing from SDS gels is discussed.

ErythrocytesSodiumLysineBiophysicschemistry.chemical_elementBiochemistryHistoneschemistry.chemical_compoundElectrochemistryAnimalsSodium dodecyl sulfateMolecular BiologyPolyacrylamide gel electrophoresisGel electrophoresisChromatographyMolecular massReproducibility of ResultsSodium Dodecyl SulfateAcetylationCell BiologyBlood Protein ElectrophoresisElectrophoresischemistryBiochemistryAcetylationElectrophoresis Polyacrylamide GelChickensAnalytical Biochemistry
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Exposure to malondialdehyde induces an early redox unbalance preceding membrane toxicity in human erythrocytes.

2002

This work investigated the oxidative injury to human red blood cells (RBCs) by the exposure to exogenous malondialdehyde (MDA), in a physiological environment. When a 10% RBC suspension was incubated in autologous plasma, in the presence of 50 microM MDA, 30% of MDA entered into the cells. A time-course study showed that MDA caused early (30-120 min) and delayed (3-18 h) effects. MDA caused a fast depletion of reduced glutathione, and loss of the glucose-6-phosphate dehydrogenase activity, followed by a decrease of HbO2. Accumulation of methemoglobin, and formation of small amounts of hemichrome were later evident. Also, an HbO2-derived fluorescent product was measured in the membrane. The …

ErythrocytesTime FactorsOxidative phosphorylationmedicine.disease_causeBiochemistryHemolysisMethemoglobinchemistry.chemical_compoundHemoglobinsMalondialdehydemedicineHumansMethemoglobinHemichromeCell MembraneErythrocyte MembraneGeneral MedicineGlutathionemedicine.diseaseMalondialdehydeMolecular biologyHemolysisOxygenSpectrometry FluorescencechemistryBiochemistryGlucose-6-PhosphatasePotassiumElectrophoresis Polyacrylamide GelOxidation-ReductionIntracellularOxidative stressFree radical research
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Electrophoretic separation of a class of nucleosomes enriched in HMG 14 and 17 and actively transcribed globin genes.

1980

Monomer nucleosomes from chick erythrocytes can be fractionated according to their electrophoretic mobility in (comparatively) high salt acrylamide gels. We show that the fractionation is based predominantly on differences in charge. The monomer heterogeneity persists even when the nucleosomes are trimmed down to 145 bp with Exo III or when H1 and H5 are removed. The slowest migrating monomers are associated with HMG 14 and 17; however, we do not believe that these proteins are entirely responsible for the altered mobility since the nucleosome heterogeneity persists even after removal of HMG 14 and 17. The DNA associated with the HMG 14 and 17 containing nucleosomes is shown to be enriched …

ErythrocytesbiologyChromosomal Proteins Non-HistoneHigh Mobility Group ProteinsCell FractionationNucleosomesHistoneschemistry.chemical_compoundElectrophoresisMonomerHistonechemistryBiochemistryHMG-CoA reductaseGeneticsbiology.proteinNucleosomeAnimalsElectrophoresis Polyacrylamide GelGlobinCell fractionationChickensDNA
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Neutral deoxyribonucleases of HeLa S3 cells: electrophoretic separation, characterization, substrate specificity and mode of action.

1980

Extracts of HeLa S3 cells were electrophoresed on polyacrylamide gels; gel slices were eluted and the eluates were assayed for DNase activities against native and denatured DNA substrates in the presence of MgCl2 or Na2EDTA. Aliquots of each eluate were also assayed for their ability to nick the circular supercoiled PM2 phage DNA to distinguish endonucleases from exonucleases. Peaks of endonuclease activities were characterized as forming 3′-phospho-oligonucleotides or 5′-phospho-oligonucleotides by the use of oligonucleotides produced by these enzymes as substrates for the 5′-phosphate-specific snake venom exonuclease. The total activity of DNases in gel eluates was much higher than that i…

ExonucleasePolyacrylamideDNA Single-StrandedBiochemistrySubstrate SpecificityEndonucleasechemistry.chemical_compoundHumansMagnesiumEdetic Acidchemistry.chemical_classificationChromatographyDeoxyribonucleasesbiologyOligonucleotideHydrogen-Ion ConcentrationElectrophoresisEnzymeBiochemistrychemistryDNA Viralbiology.proteinElectrophoresis Polyacrylamide GelDNA CircularDeoxyribonucleasesDNAHeLa CellsEuropean journal of biochemistry
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Development of Antioxidant Protein Extracts from Gilthead Sea Bream (Sparus aurata) Side Streams Assisted by Pressurized Liquid Extraction (PLE)

2021

The pressurized liquid extraction (PLE) technique was used, for the first time, to obtain protein extracts with antioxidant activity from side streams (muscle, heads, viscera, skin, and tailfins) of gilthead sea bream (Sparus aurata) in order to give added value to these underutilized matrices. Extraction conditions previously optimized for sea bass (Dicentrarchus labrax) side streams were applied. Protein recovery percentages were 22% (muscle), 33% (heads), 78% (viscera), 24% (skin), and 26% (tailfins), which represented an increase of 1.2–4.5-fold compared to control samples (extraction by stirring). The SDS-PAGE profiles revealed that PLE-assisted extraction influenced protein molecular …

Fish ProteinsSpectrometry Mass Electrospray IonizationAntioxidantOxygen radical absorbance capacityFood HandlingElectrospray ionizationmedicine.medical_treatmentLiquid-Liquid ExtractionTrolox equivalent antioxidant capacityPharmaceutical Scienceantioxidant capacity01 natural sciencesAntioxidantsArticle0404 agricultural biotechnologymycotoxinsDrug Discoverypressurized liquid extractionmedicinePressuregilthead sea breamAnimalsSea bassheavy metalsPharmacology Toxicology and Pharmaceutics (miscellaneous)Inductively coupled plasma mass spectrometrylcsh:QH301-705.5Chromatography High Pressure LiquidWaste ProductsChromatographyOxygen Radical Absorbance CapacitybiologyChemistryside streams010401 analytical chemistryExtraction (chemistry)04 agricultural and veterinary sciencesbiology.organism_classification040401 food scienceSea Bream0104 chemical sciencesMolecular Weightlcsh:Biology (General)MetalsDicentrarchusElectrophoresis Polyacrylamide GelproteinSDS-PAGEMarine Drugs
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TTAS a New Stilbene Derivative that Induces Apoptosis in Leishmania Infantum

2012

Leishmania parasites are able to undergo apoptosis (programmed cell death), similarly to mammalian cells. Recently it was demonstrated in vitro the anti-leishmanial effect of some natural and synthetic stilbenoids including resveratrol and piceatannol. In this study we evaluated the Leishmanicidal activity of a pool of stilbene derivatives which had previously shown high apoptotic efficacy against neoplastic cells. All the compounds tested were capable to decrease the parasite viability in a dose-dependent manner. Trans-stilbenes proved to be markedly more effective than cis-isomers. This was different from that observed in tumor cells in which cis-stilbenes were more potent cytotoxic agent…

G2 PhaseProgrammed cell deathLeishmaniasiSettore MED/17 - Malattie InfettiveImmunologyAntiprotozoal AgentsTUBULINApoptosisResveratrolChromatography AffinityLethal Dose 50chemistry.chemical_compoundGranulocyte-Macrophage Progenitor CellsAnnexin A5Leishmania infantumCytotoxicityCells CulturedMembrane Potential MitochondrialPiceatannolDose-Response Relationship DrugbiologyGeneral MedicineFlow CytometryHematopoietic Stem Cellsbiology.organism_classificationLeishmaniaPROGRAMMED CELL DEATHIn vitroInfectious DiseaseschemistryBiochemistrySTILBENESAntimony Sodium GluconateApoptosisStilbeneElectrophoresis Polyacrylamide GelParasitologyLeishmania infantumCell DivisionLEISHMANIASIS
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Modified apparatus for voltage gradient gel electrophoresis.

1999

We built a modified version of voltage gradient gel electrophoresis system to correct distortions in nucleic acids electrophoretic migration patterns occurring at the edges of the gel when the original voltage gradient apparatus is used. The new device allows correct fractionation of nucleic acids also when electrophoresis is performed at high voltages.

Gel electrophoresisChromatographyChemistryOrganic ChemistryAnalytical chemistryVoltage gradientGeneral MedicineFractionationEquipment DesignBiochemistryAnalytical ChemistryElectrophoresisNucleic acidPulsed-field gel electrophoresisElectrophoresis Polyacrylamide GelElectric potentialVoltageJournal of chromatography. A
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Applicability of the log MM - √D relationship to linear polyacrylamide gradient gel electrophoresis under a wide range of experimental conditions

1982

Recently we reported about a linear correlation between the logarithm of the size of native proteins (log mol mass or log Stokes' radius) and the square root of their migration distance (- √D) in linear polyacrylamide (PAA)-gradient gels (G. M. Rothe and H. Purkhanbaba, Electrophoresis 1982, 3, 33–42). The linearity between log MM and √D is not subject to time using homogeneous buffers in electrophoresis, no matter how the constants of the corresponding regression lines, slope and intercept change as a function of time. The realiability of this correlction has been re-examined with 0.7 mm thin gel plates and extending the time of electrophoresis under non-denaturating conditions from 2 to 9…

Gel electrophoresisChromatographyLogarithmChemistryClinical BiochemistryPolyacrylamideAnalytical chemistryLinearityRadiusBiochemistryAnalytical Chemistrychemistry.chemical_compoundElectrophoresisLinear regressionSodium dodecyl sulfateElectrophoresis
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Efficient Extraction of Olive Pulp and Stone Proteins by using an Enzyme-Assisted Method

2014

An efficient protein extraction protocol for proteins from olive pulp and stone by using enzymes was developed. For this purpose, different parameters that affect the extraction process, such as enzyme type and content, pH, and extraction temperature and time, were tested. The influence of these factors on protein recovery was examined using the standard Bradford assay, while the extracted proteins were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The best extraction conditions were achieved at pH 7.0 and 5% (v/v) Palatase® 20000 L (lipase) for pulp and Lecitase® Ultra (phospholipase) for stone proteins. The optimal extraction temperature and time w…

Gel electrophoresisChromatographybiologyChemistryPulp (paper)Extraction (chemistry)engineering.materialElectrophoresisProtein purificationengineeringbiology.proteinLipasePolyacrylamide gel electrophoresisBradford protein assayFood ScienceJournal of Food Science
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