Search results for "Affinity"

showing 10 items of 313 documents

Adsorption of gold clusters on metal-supported MgO: Correlation to electron affinity of gold

2007

Adsorption of ${\mathrm{Au}}_{N}$ clusters $(N=1\char21{}6)$ on a bulk MgO(001) surface and on an ultrathin (3 ML) MgO(001) film supported by Mo metal is investigated via density-functional theory calculations. Comparison of the two substrates unambiguously shows that the gold clusters adsorbed on $\mathrm{Mg}\mathrm{O}∕\mathrm{Mo}$ turn into singly charged cluster anions ${\mathrm{Au}}_{N}^{\ensuremath{\delta}}$, $\ensuremath{\delta}\ensuremath{\approx}\ensuremath{-}1$. Their structures and internal charging patterns are analogous to singly charged, planar, gas-phase cluster anions ${\mathrm{Au}}_{N}^{\ensuremath{-}}$. The adsorption energy has prominent size-dependent odd-even oscillation…

Range (particle radiation)Materials scienceCondensed Matter PhysicsElectronic Optical and Magnetic MaterialsMetalCondensed Matter::Materials ScienceCrystallographyAdsorptionvisual_artElectron affinityvisual_art.visual_art_mediumCluster (physics)Atomic physicsAdsorption energyPhysical Review B
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The N-terminal Amino Group of [Tyr8]Bradykinin Is Bound Adjacent to Analogous Amino Acids of the Human and Rat B2 Receptor

1996

To obtain data of the bradykinin B2 receptor's agonist binding site, we used a combined approach of affinity labeling and "immunoidentification" of receptor fragments generated by cyanogen bromide cleavage. Domain-specific antibodies to the various extracellular receptor domains were applied to detect receptor fragments with covalently attached [125I-Tyr8]bradykinin. As a cross-linker we used the homobifunctional reagent disuccinimidyl tartarate (DST), which reacts preferentially with primary amines. With this technique a [125I-Tyr8]bradykinin-labeled receptor fragment derived from the third extracellular domain was identified. The epsilon-amino group of lysine (Lys172) of the human B2 rece…

Receptor Bradykinin B2StereochemistryAffinity labelMolecular Sequence DataBradykininBradykininTransfectionBiochemistryProtein Structure SecondaryCell LineIodine Radioisotopeschemistry.chemical_compoundAnimalsHumansAmino Acid SequenceBradykinin receptorReceptorMolecular BiologyPeptide sequencechemistry.chemical_classificationBinding SitesAffinity labelingbiologyLysineReceptors BradykininAffinity LabelsCell BiologyRecombinant ProteinsRatsAmino acidCross-Linking ReagentschemistryBiochemistryCOS CellsFree fatty acid receptorbiology.proteinJournal of Biological Chemistry
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Adhesion of 8701-BC breast cancer cells to type V collagen and 67 kDa receptor

1992

Ductal infiltration carcinomas (d.i.c.) of the breast are potentially highly metastatic tumours, associated with drastic alterations of the architecture and molecular composition of the extracellular matrix at the tumour-host interface. 8701-BC, a recently characterized cell line, isolated from primary d.i.c., was used to study different aspects of tumor cell-substratum interactions. Since type V collagen deposition is augmented in d.i.c. we have examined the ability of 8701-BC cells to interact with this collagen species. We have found that cell binding to type V collagen was mediated by protein homologous to the 67 kDa laminin receptor (67-R). This conclusion is substantiated by the follo…

Receptors CollagenbiologyIntegrinMammary Neoplasms ExperimentalLactoseReceptors Cell SurfaceCell BiologyMolecular biologyChromatography AffinityCollagen receptorExtracellular matrixCollagen type I alpha 167 kDa Laminin ReceptorMembrane proteinCell AdhesionTumor Cells Culturedbiology.proteinAnimalsCollagenCell adhesionReceptorJournal of Cell Science
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Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase fromCandida albicans

1999

We report here the purification of a functionally active recombinant glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from Candida albicans. The GAPDH protein encoded by the TDH1 gene was obtained as a glutathione S-transferase fusion protein by expression in the vector pGEX-4T-3, and purified by affinity chromatography and thrombin digestion. The purified protein displays GAPDH enzymatic activity (42 micromol NADH min(-1) mg(-1)) as well as the laminin and fibronectin binding activities previously described. In addition, the recombinant GAPDH is covalently modified by NAD linkage; this modification is stimulated by nitric oxide and probably involves a sulfhydryl group (cysteine) residue si…

Recombinant Fusion ProteinsDehydrogenaseBiologyMicrobiologyChromatography Affinitylaw.inventionchemistry.chemical_compoundstomatognathic systemAffinity chromatographylawGlyceraldehydeCandida albicansEscherichia coliGeneticsCloning MolecularMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseGlutathione TransferaseThrombinGlyceraldehyde-3-Phosphate DehydrogenasesMolecular biologyRecombinant ProteinsKineticschemistryBiochemistryFibronectin bindingbiology.proteinRecombinant DNAGlyceraldehyde 3-phosphateCysteineFEMS Microbiology Letters
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Potential of human serum albumin as chiral selector of basic drugs in affinity electrokinetic chromatography-partial filling technique

2006

The enantiomeric resolution of compounds using HSA by means of affinity EKC (AEKC)-partial filling technique is the result of a delicate balance between different experimental variables such as protein concentration, running pH (background electrophoretic buffer (BGE), protein, and compound solutions), and plug length. In this paper, the possibility of using HSA as chiral selector for enantioseparation of 28 basic drugs using this methodology is studied. The effect of the physicochemical parameters, the structural properties of compounds, and compound-HSA protein binding percentages over their chiral resolution with HSA is outlined. Based on the results obtained, a decision tree is proposed…

Resolution (mass spectrometry)Clinical BiochemistryPlasma protein bindingBuffersBiochemistryChromatography AffinityAnalytical ChemistryElectrokinetic phenomenaMolar volumemedicineHumansSerum AlbuminChromatography Micellar Electrokinetic CapillaryChromatographyMolecular StructureChemistryStereoisomerismHydrogen-Ion ConcentrationHuman serum albuminChiral resolutionbody regionsElectrophoresisPharmaceutical Preparationsembryonic structuresEnantiomerHydrophobic and Hydrophilic Interactionsmedicine.drugELECTROPHORESIS
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Site specificity of pea histone acetyltransferase B in vitro.

1993

Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites i…

Saccharomyces cerevisiae ProteinsLysineMolecular Sequence DataBiochemistryChromatography AffinitySubstrate SpecificityHistone H4HistonesAffinity chromatographyAcetyltransferasesHistone octamerAmino Acid SequenceMolecular BiologyHistone AcetyltransferasesPlants MedicinalbiologyAcetylationFabaceaeCell BiologyHistone acetyltransferaseMolecular biologyIsoenzymesHistoneBiochemistryAcetylationHistone methyltransferasebiology.proteinElectrophoresis Polyacrylamide GelThe Journal of biological chemistry
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Mannoprotein of the yeast cell wall as primary receptor for the killer toxin of Saccharomyces cerevisiae strain 28.

1987

The killer toxin KT 28 of Saccharomyces cerevisiae strain 28 is primarily bound to the mannoprotein of the cell wall of sensitive yeasts. The mannoprotein of S. cerevisiae X 2180 was purified; gel filtration and SDS-PAGE indicated an estimated Mr of 185,000. The ability to bind killer toxin KT 28 increased during purification of the mannoprotein. Removing the protein part of the mannoprotein by enzymic digestion or removing the alkali-labile oligosaccharide chains by beta-elimination did not destroy the ability to bind killer toxin KT 28. However, binding activity was lost when the 1,6-alpha-linkages of the outer carbohydrate backbone were hydrolysed by acetolysis. The separated oligomannos…

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologymedicine.disease_causeMicrobiologyChromatography AffinityCell wallSepharoseAffinity chromatographyCell WallmedicineReceptorGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsToxinOligosaccharideMycotoxinsbiology.organism_classificationChromatography Ion ExchangeYeastKiller Factors Yeastcarbohydrates (lipids)chemistryBiochemistryAdsorptionJournal of general microbiology
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Bio-affinity of MC3T3-E1 osteoblastic cells with polymeric scaffold in Poly L-Lactid Acid (PLLA) for bone substitution.

2009

Damage to an organ or tissue remains a problem despite advances in medical technology. Available treatments include organs transplantation, surgical reconstruction such as mechanical devices. However, all these methodologies have several contraindications. In recent years, tissue engineering methods is considered as means to replace diseased or damaged organs. For these kind of application, the choice of scaffolding material is crucial to the success of the technique. In the function of the application, the synthetic scaffolds should meet several criteria, including: good biocompatibility, sufficient mechanical properties, and adequate biodegradability. The aim of our study was to evaluate …

ScaffoldBio-affinityOsteoblastic cellSettore BIO/10 - BiochimicaPLLA
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Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum.

2007

A novel fucose-binding lectin, designated SauFBP32, was purified by affinity chromatography on fucose-agarose, from the serum of the gilt head bream Sparus aurata. Electrophoretic mobility of the subunit revealed apparent molecular weights of 35 and 30 kDa under reducing and non-reducing conditions, respectively. Size exclusion analysis suggests that the native lectin is a monomer under the selected experimental conditions. Agglutinating activity towards rabbit erythrocytes was not significantly modified by addition of calcium or EDTA; activity was optimal at 37 degrees C, retained partial activity by treatment at 70 degrees C, and was fully inactivated at 90 degrees C. On western blot anal…

Serum hemagglutininsTeleostMolecular Sequence DataBiophysicsBiochemistryAffinity chromatographyWestern blotSparus aurataLectinsmedicineAnimalsDicentrarchus labraxAmino Acid SequenceSea bassMolecular BiologyPeptide sequencePolyacrylamide gel electrophoresisbiologyMolecular massmedicine.diagnostic_testSequence Homology Amino AcidLectinF-type lectin; Sparus aurata; Dicentrarchus labrax; Teleost; Serum hemagglutininsbiology.organism_classificationSea BreamBiochemistrybiology.proteinChromatography GelDicentrarchusElectrophoresis Polyacrylamide GelF-type lectinBiochimica et biophysica acta
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A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax

2001

A lectin specific for fucose and galactose was isolated by affinity chromatography on Sepharose CL-6B from the serum of Dicentrarchus labrax. The hemagglutinating activity against rabbit erythrocytes was calcium-independent, and reached its maximum at 37 degrees C. Two protein components were found in the hemagglutinating fractions eluted from the Sepharose column. Only the 34 kDa component (DLL2) eluted from the polyacrylamide gels (SDS-PAGE) showed agglutinating activity against rabbit erythrocytes. SDS-PAGE, in non-reducing conditions, revealed a single 66 kDa protein that reacted with antibodies to the 34 kDa component. Therefore, a dimeric structure stabilized by disulfide bonds can be…

SerumImmunoblottingCarbohydratesSettore BIO/05 - ZoologiaBiophysicsHemagglutinin (influenza)CentrifugationBiochemistryFucoseSepharosechemistry.chemical_compoundAffinity chromatographyLectinsAnimalsDicentrarchus labraxHemagglutininSea bassMolecular BiologybiologyLectinHemagglutination Testsbiology.organism_classificationFishchemistryBiochemistryGalactosebiology.proteinBassElectrophoresis Polyacrylamide GelDicentrarchusFucolectinBiochimica et Biophysica Acta (BBA) - General Subjects
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