Search results for "Poly(acrylamide)"

showing 10 items of 377 documents

A Newly-Detected Reductase fromRauvolfiaCloses a Gap in the Biosynthesis of the Antiarrhythmic Alkaloid Ajmaline

2002

A new enzyme, 1,2-dihydrovomilenine reductase (E.C. 1.3.1), has been detected in Rauvolfia cell suspension cultures. The enzyme specifically converts 2beta( R)-1,2-dihydrovomilenine through an NADPH-dependent reaction into 17-O-acetylnorajmaline, a close biosynthetic precursor of the antiarrhythmic alkaloid ajmaline from Rauvolfia. A five-step purification procedure using SOURCE 30Q chromatography, hydroxyapatite chromatography, 2',5'-ADP Sepharose 4B affinity chromatography and ion exchange chromatography on DEAE Sepharose and Mono Q delivered an approximately 200-fold enriched enzyme in a yield of approximately 6%. SDS-PAGE showed an M r for the enzyme of approximately 48 kDa. Optimum pH …

Oxidoreductases Acting on CH-CH Group DonorsRauvolfiaIon chromatographyPharmaceutical ScienceReductaseRauwolfiaAnalytical ChemistrySepharosechemistry.chemical_compoundAffinity chromatographyDrug DiscoverymedicineHumansChromatography High Pressure LiquidPharmacologychemistry.chemical_classificationAjmalinebiologyOrganic Chemistrybiology.organism_classificationAjmalineEnzymeComplementary and alternative medicinechemistryDEAE-SepharoseBiochemistryMolecular MedicineElectrophoresis Polyacrylamide GelOxidoreductasesAnti-Arrhythmia AgentsPhytotherapymedicine.drugPlanta Medica
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Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocatio…

2006

The role of cysteines 449 (Cys449) and 459 (Cys459) from the large subunit (LS) of ribulose 1-5-bisphosphate carboxylase/oxygenase (Rubisco) in the reduction-oxidation (redox) regulation of the enzyme was assessed by site-directed mutagenesis of these residues and chloroplast transformation of Chlamydomonas reinhardtii. In vitro studies indicated that mutations C449S, C459S or C449S/ C459S do not affect the activity and proteolytic susceptibility of the enzyme in the reduced state. However, when oxidized, the mutant enzymes differed from the wild type (WT), showing an increased resistance to inactivation and, in the case of the double mutant (DM), an altered structural conformation as refle…

OxygenaseProtein ConformationPhysiologyRibulose-Bisphosphate CarboxylaseBlotting WesternChlamydomonas reinhardtiiPlant ScienceBiologychemistry.chemical_compoundCysteinechemistry.chemical_classificationRibulose 15-bisphosphateRibuloseCell MembraneRuBisCOWild typebiology.organism_classificationPyruvate carboxylaseProtein TransportEnzymeBiochemistrychemistryMutagenesis Site-Directedbiology.proteinElectrophoresis Polyacrylamide GelOxidation-ReductionPlant, Cell and Environment
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The nucleus negatively controls the synthesis of mitochondrial proteins in the sea urchin egg.

1983

Enucleation of Paracentrotus lividus eggs, followed by parthenogenetic activation induces a sharp increase in the synthesis of mitochondrial proteins as shown by electrofluorography after in vivo labeling with radioactive amino acids. These results further substantiate the hypothesis that the cell nucleus negatively controls mitochondrial replication in the sea urchin egg.

ParthenogenesisBiologyParacentrotus lividusbiology.animalmedicineProtein biosynthesisAnimalsAmino AcidsSea urchinPolyacrylamide gel electrophoresisOvumchemistry.chemical_classificationCell NucleusProteinsCell BiologyParthenogenesisAnatomybiology.organism_classificationAmino acidCell biologyMitochondriaCell nucleusmedicine.anatomical_structurechemistryProtein BiosynthesisSea Urchinsembryonic structuresElectrophoresis Polyacrylamide GelFemaleNucleusCell biology international reports
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Primary structure and unusual carbohydrate moiety of functional unit 2-c of keyhole limpet hemocyanin (KLH)

1999

Abstract The complete amino acid sequence of the Megathura crenulata hemocyanin functional unit KLH2-c was determined by direct sequencing and matrix-assisted laser desorption ionization mass spectrometry of the protein, and of peptides obtained by cleavage with EndoLysC proteinase, chymotrypsin and cyanogen bromide. This is the first complete primary structure of a functional unit c from a gastropod hemocyanin. KLH2-c consists of 420 amino acid residues. Circular dichroism spectra indicated approx. 31% β-sheet and 29% α-helix contents. A multiple sequence alignment with other molluscan hemocyanin functional units revealed average identities between 41 and 49%, but 55% in case of Octopus he…

Peanut agglutininmedicine.medical_treatmentMolecular Sequence DataCarbohydratesBiophysicschemical and pharmacologic phenomenaMegathura crenulataBiochemistrychemistry.chemical_compoundStructural BiologymedicineAnimalsChymotrypsinAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceChromatography High Pressure LiquidbiologyMolecular massCircular DichroismProtein primary structureHemocyaninbiology.organism_classificationMolecular WeightBiochemistrychemistryMolluscaSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationHemocyaninsbiology.proteinElectrophoresis Polyacrylamide GelCyanogen bromideSequence AlignmentKeyhole limpet hemocyaninBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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Core-Shell Microgels with Switchable Elasticity at Constant Interfacial Interaction.

2016

Hydrogels based on poly(N-isopropylacrylamide) (pNIPAAm) exhibit a thermo-reversible volume phase transition from swollen to deswollen states. This change of the hydrogel volume is accompanied by changes of the hydrogel elastic and Young's moduli and of the hydrogel interfacial interactions. To decouple these parameters from one another, we present a class of submillimeter sized hydrogel particles that consist of a thermosensitive pNIPAAm core wrapped by a nonthermosensitive polyacrylamide (pAAm) shell, each templated by droplet-based microfluidics. When the microgel core deswells upon increase of the temperature to above 34 °C, the shell is stretched and dragged to follow this deswelling i…

Phase transitionMaterials scienceAtomic force microscopyMicrofluidicsPolyacrylamideModulus02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciences0104 chemical sciencesCore shellchemistry.chemical_compoundchemistrySelf-healing hydrogelsGeneral Materials ScienceComposite materialElasticity (economics)0210 nano-technologyACS applied materialsinterfaces
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PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
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Properties of baculovirus particles displaying GFP analyzed by fluorescence correlation spectroscopy.

2003

Abstract Recombinant baculovirus particles displaying green fluorescent protein (GFP) fused to the major envelope glycoprotein gp64 of the Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) were characterized by fluorescence correlation spectroscopy (FCS). FCS detected Brownian motion of single, intact recombinant baculovirus display particles with a diffusion coefficient (D) of (2.89±0.74)10 8 cm2s 1 and an apparent hydrodynamic radius of 83.35±21.22 nm. In the presence of sodium dodecyl sulfate (SDS), Triton X-100, and octylglucoside, the diffusion time was reduced to the 0.2 ms range (D = 7.5710 7 cm2s 1), showing that the fusion proteins were anchored in the viral envelope…

PhotochemistryvirusesClinical BiochemistryDetergentsGreen Fluorescent ProteinsFluorescence correlation spectroscopySpodopteraBiochemistryGreen fluorescent proteinDiffusionchemistry.chemical_compoundViral envelopeAnimalsSodium dodecyl sulfateMolecular BiologybiologyChemistryViral membranebiology.organism_classificationFluorescenceFusion proteinMolecular biologyMolecular WeightAutographa californicaLuminescent ProteinsSpectrometry FluorescenceElectrophoresis Polyacrylamide GelIndicators and ReagentsBaculoviridaeViral Fusion ProteinsAlgorithmsBiological chemistry
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Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus.

2000

When Astacus leptodactylus were kept at various temperatures for several weeks, different ratios between di-hexameric and hexameric hemocyanins were observed in their hemolymph. The higher the temperature the more hexamers were present. This long-term adaptation to different temperatures or/and to temperature-induced pH-shifts as observed in the hemolymph has different effects on the expression of subunit types building up hexamers and those which covalently link two hexamers within the di-hexamers. The oxygen binding behaviour of di-hexameric hemocyanins from cold and warm adapted animals do not show differences with respect to affinity, Bohr effect and cooperativity.

PhysiologyEcologymedicine.medical_treatmentProtein subunitTemperatureCooperativityHemocyaninBohr effectmacromolecular substancesBiologyHydrogen-Ion ConcentrationAstacus leptodactylusbiology.organism_classificationBiochemistryAdaptation PhysiologicalCrustaceaHemolymphHemocyaninsmedicineBiophysicsAnimalsElectrophoresis Polyacrylamide GelAdaptationMolecular BiologyOxygen bindingComparative biochemistry and physiology. Part A, Molecularintegrative physiology
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Biosilicification of loricate choanoflagellate: organic composition of the nanotubular siliceous costal strips of Stephanoeca diplocostata.

2010

SUMMARY Loricate choanoflagellates (unicellular, eukaryotic flagellates; phylum Choanozoa) synthesize a basket-like siliceous lorica reinforced by costal strips (diameter of approximately 100 nm and length of 3 μm). In the present study, the composition of these siliceous costal strips is described, using Stephanoeca diplocostata as a model. Analyses by energy-dispersive X-ray spectroscopy (EDX), coupled with transmission electron microscopy (TEM), indicate that the costal strips comprise inorganic and organic components. The organic, proteinaceous scaffold contained one major polypeptide of mass 14 kDa that reacted with wheat germ agglutinin. Polyclonal antibodies were raised that allowed …

PhysiologyLoricate choanoflagellateBiosilicificationNanotechnologyStructural analysisOrganic compositionAquatic ScienceAlkaliesStephanoeca diplocostataHydrofluoric AcidBiosilicification; Loricate choanoflagellate; Organic composition; Structural analysisAnimalsChemical PrecipitationOrganic ChemicalsChoanoflagellateMolecular BiologyEcology Evolution Behavior and SystematicsChoanoflagellatabiologyChemistryAnimal StructuresProteinsSpectrometry X-Ray Emissionbiology.organism_classificationElementsSilicon DioxideImmunohistochemistryWheat germ agglutininNanostructuresSolutionsElectrophoresisTransmission electron microscopyInsect ScienceBiophysicsAnimal Science and ZoologyComposition (visual arts)Electrophoresis Polyacrylamide GelLorica (biology)ChoanozoaThe Journal of experimental biology
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Dynamic electric field assisted multi-dimensional liquid chromatography of biological samples

2005

Complex biological samples require very high resolution separation strategies. The platform introduced here capitalises on the hyphenation of liquid chromatographic (LC) and electric potential gradient electrochromatographic multi-dimensional separation genres. First-dimension selectivity is provided by simultaneous size exclusion (SEC) and strong cation exchange (SCX) chromatography modes, while the second dimension comprises reversed phase (RP) characteristics in a dynamic (time-variant) electric field. The time-variant potential gradient with reversal of polarity is applied across the second dimension monolithic capillary throughout the duration of the solvent strength gradient elution. …

Polarity reversalAnalyteChromatographyChemistryClinical BiochemistrySize-exclusion chromatographyAnalytical chemistryCell BiologyGeneral MedicineReversed-phase chromatographyChromatography Ion ExchangeSensitivity and SpecificityBiochemistryAnalytical ChemistryMatrix (chemical analysis)Electric fieldPotential gradientChromatography GelHumansElectrophoresis Polyacrylamide GelElectric potentialBlood Chemical AnalysisJournal of Chromatography B
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