Search results for "Base Sequence"

showing 10 items of 1146 documents

Phosphorylation of the Goodpasture antigen by type A protein kinases.

1995

Collagen IV is the major component of basement membranes. The human alpha 3 chain of collagen IV contains an antigenic domain called the Goodpasture antigen that is the target for the circulating immunopathogenic antibodies present in patients with Goodpasture syndrome. Characteristically, the gene region encoding the Goodpasture antigen generates multiple alternative products that retain the antigen amino-terminal region with a five-residue motif (KRGDS). The serine therein appears to be the major in vitro cAMP-dependent protein kinase phosphorylation site in the isolated antigen and can be phosphorylated in vitro by two protein kinases of approximately 50 and 41 kDa associated with human …

inorganic chemicalsCollagen Type IVAnti-Glomerular Basement Membrane DiseaseMolecular Sequence DataBiochemistryAutoantigensSerineAntigenmedicineSerineGoodpasture syndromeHumansAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyBasement membranebiologyBase SequenceKinaseCell Biologymedicine.diseaseMolecular biologyCyclic AMP-Dependent Protein Kinasesenzymes and coenzymes (carbohydrates)medicine.anatomical_structureOligodeoxyribonucleotidesbiology.proteinPhosphorylationCollagenAntibodyThe Journal of biological chemistry
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Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis.

2008

Abstract Background The interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions. Results Purifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the e…

lcsh:Animal biochemistryMESH : AgedMESH : RodentiaMESH: RodentiaMESH: Base SequenceBiochemistryMESH: Lipid PeroxidationMESH : Information ServicesAntigen-Antibody ReactionsMESH: Health EducationEpitopesMESH: OrganizationsMESH: LibrariesMESH: Antigen-Antibody Reactionslcsh:QD415-436MESH: AnimalsMESH : OrganizationsMESH : Physician's RoleMESH: Bacterial ProteinsImmunosorbent Techniqueschemistry.chemical_classificationMESH: Conserved SequenceMethodology ArticleMESH : Computer Communication NetworksMESH: Chromatography AffinityMESH : Pseudomonas aeruginosaMESH : Chromatography AffinityMESH : Immunosorbent TechniquesMESH: Ethnic GroupsMESH : Ethnic GroupsMESH: EpitopesMESH : Patient SatisfactionMESH : United StatesMESH: MitochondriaMESH : Antigen-Antibody ReactionsMolecular Sequence DataMESH : Hydroxybutyrate DehydrogenaseMESH: Sequence AlignmentRodentiaMESH: Information ServicesMESH : Epitopeslcsh:BiochemistryMESH : Mitochondrial MembranesBacterial ProteinsMESH : Conserved SequenceComplementary DNAMESH : LibrariesMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Immunosorbent TechniquesMESH: Molecular Sequence DataMESH: HumansMESH : Consumer ParticipationMESH : HumansMESH: AdultMESH: Patient SatisfactionMESH: Hydroxybutyrate DehydrogenaseMESH: Consumer ParticipationchemistryLipid PeroxidationMESH: FemaleMESH: LiverMESH : Sequence Analysis DNAMESH: Continental Population GroupsMESH: Sequence Analysis DNAMESH : Molecular Sequence DataDehydrogenaseChromatography AffinityMESH: Mitochondrial MembranesMESH: Antibodies BacterialMESH : Bacterial ProteinsMESH : FemaleMESH: Computer Communication NetworksConserved SequenceMESH: AgedbiologyMESH : Lipid PeroxidationMESH : Sequence AlignmentMESH: Physician's RoleMESH : AdultAntibodies BacterialMitochondriaAmino acidLiverBiochemistryMitochondrial MembranesPseudomonas aeruginosaMESH: Pseudomonas aeruginosaMESH : MitochondriaMESH : Mass MediaMESH: Mass MediaMESH : MaleHydroxybutyrate DehydrogenaseAffinity chromatographyMESH : Health Education[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: United StatesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Antibodies Bacteriallcsh:QP501-801Jaculus orientalisMESH : Continental Population GroupsBase SequenceMESH : LiverSequence Analysis DNAbiology.organism_classificationMolecular biologyMESH: MaleEnzymePolyclonal antibodiesbiology.proteinMESH : Base SequenceNAD+ kinaseMESH : AnimalsSequence Alignment
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Expression and characterization of the recombinant juvenile hormone epoxide hydrolase (JHEH) from Manduca sexta.

1998

The cDNA of the microsomal Juvenile Hormone Epoxide Hydrolase (JHEH) from Manduca sexta was expressed in vitro in the baculovirus system. In insect cell culture, the recombinant enzyme (Ms-JHEH) was produced at a high level (100 fold over background EH catalytic activity). As expected, Ms-JHEH was localized in the microsomal fraction with a molecular mass of approximately 50 kDa. Ms-JHEH showed a substrate and inhibitor spectrum similar to the wild type JHEH isolated from eggs of M. sexta. Its enzymatic activity was the highest for Juvenile Hormone III. Ms-JHEH hydrolyzed several trans-epoxides faster than cis-epoxides. A putative hydroxyl-acyl enzyme intermediate was isolated suggesting a …

mechanismGene ExpressionBiochemistryPolymerase Chain ReactionSubstrate SpecificityManduca sextaManducaHydrolaseAnimalsEpoxide hydrolaserecombinant enzymeMolecular BiologyDNA Primerschemistry.chemical_classificationEpoxide HydrolasesbiologyMolecular massBase Sequencejuvenile hormoneInsect cell cultureHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyRecombinant Proteinsepoxide hydrolaseJuvenile HormonesEnzymechemistryBiochemistryManduca sextaInsect ScienceJuvenile hormoneManducaBaculoviridaeInsect biochemistry and molecular biology
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Patterns and rates of nucleotide substitution, insertion and deletion in the endosymbiont of antsBlochmannia floridanus

2009

Genome reduction is a general process that has been studied in numerous symbiotic bacteria associated with insects. We investigated the last stages of genome degradation in Blochmannia floridanus, a mutualistic bacterial endosymbiont of the ant Camponotus floridanus. We determined the tempo (rates of insertion and deletion) and mode (size and number of insertion-deletion events) of the process in the last 200,000 years by analysing a total of 16 intergenic regions in several strains of this endosymbiont from different ant populations. We provide the first calculation of the reduction rate for noncoding DNA in this endosymbiont (2.2 x 10(-8) lost nucleotides/site/year) and compare it with th…

medicine.disease_causePolymerase Chain ReactionPolymorphism Single NucleotideGenomeIntergenic regionGeneticsmedicineAnimalsSymbiosisIndelEscherichia coliEcosystemPhylogenyEcology Evolution Behavior and SystematicsSequence DeletionGeneticsGenomeBase SequencebiologyAntsbiology.organism_classificationNoncoding DNADNA Transposable ElementsFloridaMicrosatelliteCamponotus floridanusBuchneraMolecular Ecology
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Domains of the E1 Protein of Human Papillomavirus Type 33 Involved in Binding to the E2 Protein

1996

Papillomavirus E1 and E2 proteins are essential for the initiation of viral DNA replication. We have now analyzed the interaction of E1 and E2 of human papillomavirus type 33, which is associated with cervical carcinoma. When synthesized in insect cells using the baculovirus expression system, the E1 and E2 proteins interacted efficiently at 4 degree. A monoclonal antibody recognizing E1 amino acids 584--600 inhibited the binding of E2 and vice versa, indicating that these amino acids are involved in E2 binding. To confirm this result, a mutational analysis of E1 was performed. The E2 binding activity of E1 deletion and point mutant proteins was assayed using glutathione S-transferase E1 fu…

medicine.drug_classRecombinant Fusion ProteinsMolecular Sequence DataContext (language use)BiologySpodopteraMonoclonal antibodyAntibodies ViralCell Linechemistry.chemical_compoundMiceVirologymedicineTumor Cells CulturedAnimalsHumansPoint MutationPapillomaviridaeDNA PrimersGlutathione TransferaseSequence Deletionchemistry.chemical_classificationMice Inbred BALB CBase SequencePoint mutationTemperatureAntibodies MonoclonalGlutathioneOncogene Proteins ViralFusion proteinMolecular biologyIn vitroAmino acidchemistryEpitope MappingBinding domainProtein BindingVirology
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Analysis of type-restricted and cross-reactive epitopes on virus-like particles of human papillomavirus type 33 and in infected tissues using monoclo…

1994

A panel of six monoclonal antibodies recognizing at least three different antigenic regions has been raised against the L1 major capsid protein of human papillo-mavirus type 33 (HPV-33), which is associated with cervical carcinoma. The antigenic sites defined by these antibodies have been mapped and classified as type-restricted or broadly cross-reactive using bacterially expressed L1 fusion proteins of a variety of HPV types. Conformational and linear epitopes have been distinguished using native and denatured virus-like particles. HPV infection of genital lesions has been analysed using both monoclonal antibodies and DNA amplification by PCR. The antibodies obtained should be useful to pr…

medicine.drug_classRecombinant Fusion ProteinsMolecular Sequence DataUterine Cervical NeoplasmsCross ReactionsAntibodies ViralMonoclonal antibodyEpitopeVirusCapsidAntigenAntibody SpecificityVirologyEscherichia colimedicineHumansAmino Acid SequenceCloning MolecularAntigens ViralPapillomaviridaeBase SequencebiologyVirionHPV infectionAntibodies MonoclonalUterine Cervical Dysplasiamedicine.diseaseFusion proteinVirologyMolecular biologyCapsidCondylomata AcuminataDNA Viralbiology.proteinFemaleAntibodySequence AlignmentEpitope MappingJournal of General Virology
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Short synthetic CDR-peptides forming the antibody combining site of the monoclonal antibody against RNA bacteriophage fr neutralize the phage activit…

1996

The construction of a mouse hybridoma FRS2 secreting neutralizing monoclonal antibody specific for RNA bacteriophages fr, MS2 and GA is reported. The genes encoding the variable domains of the monoclonal antibody FRS2 heavy and light chains were cloned and sequenced and the corresponding complementarity determining region (CDR) peptides were chemically synthesized. The CDR-peptides were tested for their ability to neutralize the activity of RNA phage fr and related RNA phages MS2 and GA. The CDR-derived peptides H2, L2 and L3 interacted with the fr phage particles and neutralized fr phage activity. Two of these peptides-H2 and L3 also had the ability to neutralize partly the activity of rel…

medicine.drug_classvirusesImmunologyMolecular Sequence DataImmunoglobulin Variable Regionchemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayComplementarity determining regionRNA PhagesMonoclonal antibodyBacteriophageMiceAntigenNeutralization TestsBacteriophage MS2medicineImmunology and AllergyAnimalsAmino Acid SequenceCloning MolecularMicroscopy ImmunoelectronMice Inbred BALB CbiologyBase SequenceRNAAntibodies MonoclonalGeneral MedicineRNA Phagesbiology.organism_classificationMolecular biologyPeptide Fragmentsbiology.proteinAntibodyHuman antibodies and hybridomas
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Effects of endocrine disruptors on genes associated with 17 beta-estradiol metabolism and excretion

2008

International audience; In order to provide a global analysis of the effects of endocrine disruptors on the hormone cellular bioavailability, we combined 17 beta-estradiol (E2) cellular flow studies with real-time PCR and Western blot expression measurements of genes involved in the hormone metabolism and excretion. Three endocrine disruptors commonly found in food were chosen for this study, which was conducted in the estrogen receptor (ER) negative hepatoblastoma HepG2 cell line: bisphenol A (BPA), genistein (GEN) and resveratrol (RES). We showed that 24h after a single dose treatment with genistein, resveratrol or bisphenol A, the expression of ATP-binding cassette transporters (the mult…

medicine.medical_specialtyATP-BINDING CASSETTE TRANSPORTERS[SDV]Life Sciences [q-bio]Clinical BiochemistryBlotting WesternEstrogen receptorGenistein010501 environmental sciencesBiologyPharmacologyResveratrol01 natural sciencesBiochemistryCell LineENDOCRINE DISRUPTORS03 medical and health scienceschemistry.chemical_compoundEndocrinologyInternal medicineUDP-GLUCURONOSYLTRANFERASEmedicineHumansHormone metabolismRNA MessengerMolecular Biology030304 developmental biology0105 earth and related environmental sciencesDNA PrimersPharmacology0303 health sciencesBase SequenceEstradiolReverse Transcriptase Polymerase Chain ReactionMultidrug resistance-associated protein 2Organic ChemistrySULFOTRANSFERASEEndocrinologyEndocrine disruptorchemistryGene Expression Regulation13. Climate actionESTRADIOL METABOLISMMultidrug Resistance-Associated Proteinshormones hormone substitutes and hormone antagonistsHormone
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The Activation Pattern of the Antioxidant Enzymes in the Right Ventricle of Rat in Response to Pressure Overload is of Heart Failure Type

2003

In the left ventricle subjected to pressure overload activity, the antioxidant enzymes increased at the hyperfunctional stage. During the transition to heart failure, these enzymes are down-regulated, oxidative stress increases, and apoptosis progresses. Maladaptative activation of the antioxidant enzymes at an early stage may contribute to the intrinsic vulnerability of right ventricle to pressure overload. The authors studied changes in expression and activity of the enzymes manganese and copper-zinc superoxide dismutases, glutathione peroxidase, and catalase in the right ventricle of rat following induction of pulmonary hypertension by injection of monocrotaline. Increase in the manganes…

medicine.medical_specialtyAntioxidantHeart Ventriclesmedicine.medical_treatmentmedicine.disease_causeAntioxidantsSuperoxide dismutaseInternal medicinePressuremedicineAnimalsRats WistarHeart Failurechemistry.chemical_classificationPressure overloadGlutathione PeroxidaseBase SequenceHypertrophy Right VentricularbiologySequence Analysis RNASuperoxide Dismutasebusiness.industryGlutathione peroxidaseCatalasemedicine.diseasePulmonary hypertensionRatsOxidative Stressmedicine.anatomical_structureEndocrinologychemistryVentricleHeart failureModels Animalbiology.proteinCardiologyReactive Oxygen SpeciesCardiology and Cardiovascular MedicinebusinessOxidative stressHeart Disease
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Cationic lipide mediated transfer of c-abl and bcr antisense oligonucleotides to immature normal myeloid cells: Uptake, biological effects and modula…

1996

Uptake and biochemical and biological effects of antisense oligodeoxynucleotides (ODN) specific for c-abl and bcr genes were studied in normal immature myeloid cells. CD34-positive cells were purified by positive and negative selection and cultured in liquid culture for 7 days. These cells were then incubated with ODNs, either alone or in combination with cationic lipids. The uptake of ODNs was enhanced by the use of cationic lipids. In addition, very low concentrations of ODNs in combination with cationic lipids were capable of specifically inhibiting the expression of the c-abl gene. In contrast, no effects were seen on the expression of bcr. However, despite the effective blocking of c-a…

medicine.medical_specialtyCell Membrane PermeabilityChemical PhenomenaMolecular Sequence DataRibonuclease HAntigens CD34BiologyTransfectionPolymerase Chain ReactionCationsProto-Oncogene Proteinshemic and lymphatic diseasesInternal medicineGene expressionmedicineHumansCation Exchange ResinsRNA NeoplasmProto-Oncogene Proteins c-ablGeneCells CulturedOncogene ProteinsABLHematologyBase SequenceCell-Free SystemChemistry PhysicalCell growthCationic polymerizationbreakpoint cluster regionBiological Transporthemic and immune systemsHematologyGeneral MedicineOligonucleotides AntisenseProtein-Tyrosine Kinasesrespiratory systemHematopoietic Stem CellsLipidsMolecular biologyHaematopoiesisGene Expression RegulationDepression ChemicalLiposomesProto-Oncogene Proteins c-bcrAnnals of Hematology
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