0000000000413979

AUTHOR

Dunja Lukovic

0000-0002-4055-4927

showing 6 related works from this author

Concentration dependent effects of commonly used pesticides on activation versus inhibition of the quince (Cydonia Oblonga) polyphenol oxidase

2009

Polyphenol oxidase (PPO) catalyzes the oxidation of o-diphenols to their respective quinones which undergo autopolymerization and form dark pigments. The interaction of PPO with various substrates and effectors remains the focus of intensive investigations due to the enzyme's key role in pigments biosynthesis including animal melanogenesis and fruit/fungi enzymatic browning. In this study, the effect of a range of commonly used pesticides on the enzyme activity has been evaluated using the purified quince (Cydonia oblonga Miller) PPO. The biochemical analysis showed that, in the presence of high pesticide concentrations, the enzyme was competitively inhibited, particularly with benomyl, car…

Models MolecularProtein ConformationMolecular Sequence DataCrystallography X-RayToxicologyPolyphenol oxidasechemistry.chemical_compoundCarbarylParathion methylAmino Acid SequenceEnzyme InhibitorsIpomoea batatasPesticidesCatechol oxidaseRosaceaeDose-Response Relationship DrugbiologyReverse Transcriptase Polymerase Chain ReactionComputational BiologyGeneral MedicineNucleic acid amplification techniqueEnzyme assayEnzyme ActivationKineticsParathionchemistryBiochemistryPolyphenolFruitbiology.proteinElectrophoresis Polyacrylamide GelNucleic Acid Amplification TechniquesCatechol OxidaseFood ScienceFood and Chemical Toxicology
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Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C):Structure and surface activity

2006

  Udgivelsesdato: 2006-Apr Surfactant protein C (SP-C) is an essential component for the surface tension-lowering activity of the pulmonary surfactant system. It contains a valine-rich alpha helix that spans the lipid bilayer, and is one of the most hydrophobic proteins known so far. SP-C is also an essential component of various surfactant preparations of animal origin currently used to treat neonatal respiratory distress syndrome (NRDS) in preterm infants. The limited supply of this material and the risk of transmission of infectious agents and immunological reactions have prompted the development of synthetic SP-C-derived peptides or recombinant humanized SP-C for inclusion in new prepar…

BioquímicaRecombinant membrain proteinSurface PropertiesSize-exclusion chromatographyMolecular Sequence DataPhospholipidBiophysicsBiologyBiochemistrylaw.inventionchemistry.chemical_compoundAffinity chromatographyPulmonary surfactantMembranes (Biologia)lawAnimalsHumansPulmonary surfactant-associated protein CAmino Acid SequenceLipid bilayerConserved SequencePhospholipidsMammalsDrug CarriersChromatographySequence Homology Amino AcidSP-CProteïnes de membranaSurfactant protein CPulmonary surfactantCell BiologyPulmonary Surfactant-Associated Protein CRecombinant ProteinsKineticschemistryBiochemistryRecombinant DNALipid-protein interactionPeptidesSequence Alignment
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Recombinant production and characterization of surfactant protein C (SP-C)

2007

La proteina SP-C forma parte del surfactante pulmonar, una mezcla de lípidos y proteínas que recubre los alvéolos, indispensable para la respiración. la SP-C e5 un componente crítico en las preparaciones usadas para el tratamiento del sindrome de distrés respiratorio en los fetos prematuros. El objetivo principal de esta tesis ha sido la puesta a punto de un nuevo método de producción de la proteína SP-C, mediante tecnología recombinante que podría servir como base para la obtención de nuevos surfactantes sintéticos, asi como una herramienta inmejorable en la cararterización de determinantes estructura-función con el objetivo último de intentar mejorar las propiedades tensio…

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Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif

2005

AbstractThe principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix–helix association and/or d…

Protein FoldingRecombinant Fusion ProteinsAmino Acid MotifsMolecular Sequence DataBiophysicsBiochemistryMicelleHydrophobic mismatchHydrophobic mismatchStructural BiologyLeucineHelix packingGeneticsGlycophorinAnimalsHumansAmino Acid SequenceGlycophorinsMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationbiologyChemistryGlycophorin AProteïnes de membranaMembrane ProteinsMembrane protein associationCell BiologyTransmembrane proteinAmino acidTransmembrane domainBiochemistryMembrane proteinMutationTransmembrane helixBiophysicsbiology.proteinPeptidesDimerizationHydrophobic and Hydrophilic Interactions
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Synthetic Pulmonary Surfactant Preparations: New developments and future trends

2008

Pulmonary surfactant is a lipid-protein complex that coats the interior of the alveoli and enables the lungs to function properly. Upon its synthesis, lung surfactant adsorbs at the interface between the air and the hypophase, a capillary aqueous layer covering the alveoli. By lowering and modulating surface tension during breathing, lung surfactant reduces respiratory work of expansion, and stabilises alveoli against collapse during expiration. Pulmonary surfactant deficiency, or dysfunction, contributes to several respiratory pathologies, such as infant respiratory distress syndrome (IRDS) in premature neonates, and acute respiratory distress syndrome (ARDS) in children and adults. The ma…

Models MolecularARDSmedicine.medical_specialtyMolecular Sequence DataAcute respiratory distressPharmacologyBiochemistryStructure-Activity RelationshipPulmonary surfactantDrug DiscoveryAnimalsHumansMedicineAmino Acid SequenceRespiratory systemPharmacologyRespiratory distressbusiness.industryOrganic ChemistryRespiratory diseasePulmonary Surfactantsmedicine.diseaseLipidsSurgeryDuring expirationBreathingMolecular MedicinebusinessProteïnesPulmons Malalties
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Interfacial behavior of recombinant forms of human pulmonary surfactant protein SP-C.

2012

The behavior at air-liquid interfaces of two recombinant versions of human surfactant protein SP-C has been characterized in comparison with that of native palmitoylated SP-C purified from porcine lungs. Both native and recombinant proteins promoted interfacial adsorption of dipalmitoylphosphatidylcholine bilayers to a limited extent, but catalyzed very rapid formation of films from different lipid mixtures containing both zwitterionic and anionic phospholipids. Once at the interface, the recombinant variants exhibited compression-driven structural transitions, consistent with changes in the orientation of the deacylated N-terminal segment, which were not observed in the native protein. Com…

Models MolecularProtein ConformationSurface PropertiesMolecular Sequence DataCatalysislaw.inventionchemistry.chemical_compoundAdsorptionPulmonary surfactantlawMoleElectrochemistryMoleculeNative proteinAnimalsHumansGeneral Materials ScienceAmino Acid SequenceSpectroscopyPhospholipidsSurfaces and InterfacesCondensed Matter PhysicsPulmonary Surfactant-Associated Protein CPeptide FragmentsRecombinant ProteinschemistryBiochemistryDipalmitoylphosphatidylcholineRecombinant DNABiophysicsLangmuir : the ACS journal of surfaces and colloids
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