Search results for "Molecular sequence"

showing 10 items of 1972 documents

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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Transfer, composition and technological characterization of the lactic acid bacterial populations of the wooden vats used to produce traditional stre…

2015

The biofilms of 12 wooden vats used for the production of the traditional stretched cheeses Caciocavallo Palermitano and PDO Vastedda della valle del Belìce were investigated. Salmonella spp. and Listeria monocytogenes were never detected. Total coliforms were at low numbers with Escherichia coli found only in three vats. Coagulase-positive staphylococci (CPS) were below the enumeration limit, whereas lactic acid bacteria (LAB) dominated the surfaces of all vats. In general, the dominance was showed by coccus LAB. Enterococci were estimated at high numbers, but usually between 1 and 2 Log cycles lower than other LAB. LAB populations were investigated at species and strain level and for thei…

Settore AGR/19 - Zootecnica SpecialeEnterococciLactococcusMolecular Sequence DataMicrobiologyMicrobiologyTechnological screeningCheeseLactic acid bacteriaAnimalsLeuconostocLactic AcidFood sciencePhylogenybiologyLactococcus lactisfood and beveragesPediococcus acidilacticiRaw milkTraditional cheesebiology.organism_classificationWoodWooden vatMilkEnterococcusLactobacillaceaeLeuconostoc mesenteroidesbacteriaCattlePediococcusEnterococci; Lactic acid bacteria; Raw milk; Technological screening; Traditional cheese; Wooden vat; Food Science; MicrobiologyEnterococcus faeciumFood ScienceSettore AGR/16 - Microbiologia Agraria
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Do island plant populations really have lower genetic variation than mainland populations? Effects of selection and distribution range on genetic div…

2015

Ecological and evolutionary studies largely assume that island populations display low levels of neutral genetic variation. However, this notion has only been formally tested in a few cases involving plant taxa, and the confounding effect of selection on genetic diversity (GD) estimates based on putatively neutral markers has typically been overlooked. Here, we generated nuclear microsatellite and plastid DNA sequence data in Periploca laevigata, a plant taxon with an island–mainland distribution area, to (i) investigate whether selection affects GD estimates of populations across contrasting habitats; and (ii) test the long-standing idea that island populations have lower GD than their mai…

Settore BIO/07 - EcologiaDNA PlantSettore AGR/05 - Assestamento Forestale E SelvicolturaRange (biology)Molecular Sequence DataSettore BIO/11 - Biologia MolecolareBiologydirectional selection island–mainland distributions microsatellites neutral markers Periploca laevigata widespread speciesGenetic variationGeneticsPeriplocaSelection GeneticEcology Evolution Behavior and SystematicsSelection (genetic algorithm)EcosystemIslandsGenetic diversityPeriplocaDirectional selectionEcologyGenetic DriftDNA ChloroplastGenetic Variationbiology.organism_classificationBiological EvolutionGenetics PopulationEvolutionary biologyGenetic LociSpainSettore BIO/03 - Botanica Ambientale E ApplicataMicrosatelliteLiterature surveyMicrosatellite Repeats
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Analysis of early strains of the norovirus pandemic variant GII.4 Sydney 2012 identifies mutations in adaptive sites of the capsid protein.

2014

AbstractGlobal surveillance for norovirus identified in 2012 the emergence of a novel pandemic GII.4 variant, termed Sydney 2012. In Italy, the novel pandemic variant was identified as early as November 2011 but became predominant only in the winter season 2012–2013. Upon sequencing and comparison with strains of global origin, the early Sydney 2012 strains were found to differ from those spreading in 2012–2013 in the capsid (ORF2) putative epitopes B, C and D, segregating into a distinct phylogenetic clade. At least three residues (333, 340 and 393, in epitopes B, C and D, respectively) of the VP1 varied among Sydney 2012 strains of different clades. These findings suggest that the spread …

Settore MED/07 - Microbiologia E Microbiologia ClinicaEvolutionMolecular Sequence DataCapsid protein VP1 epitopes Evolution GII.4 Italy Norovirus Sydney 2012 variantBiologymedicine.disease_causeEpitopeSydney 2012 variantVirologyPandemicmedicineHumansAmino Acid SequenceCladePandemicsPhylogenyPhylogenetic treeNorovirusCapsid protein VP1 epitopesVirologyGastroenteritisCapsidItalyMutationNorovirusCapsid ProteinsSeasonsWinter seasonGII.4Virology
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Epidemiological dynamics of norovirus GII.4 variant New Orleans 2009.

2015

Norovirus (NoV) is one of the major causes of diarrhoeal disease with epidemic, outbreak and sporadic patterns in humans of all ages worldwide. NoVs of genotype GII.4 cause nearly 80–90 % of all NoV infections in humans. Periodically, some GII.4 strains become predominant, generating major pandemic variants. Retrospective analysis of the GII.4 NoV strains detected in Italy between 2007 and 2013 indicated that the pandemic variant New Orleans 2009 emerged in Italy in the late 2009, became predominant in 2010–2011 and continued to circulate in a sporadic fashion until April 2013. Upon phylogenetic analysis based on the small diagnostic regions A and C, the late New Orleans 2009 NoVs circulati…

Settore MED/07 - Microbiologia E Microbiologia ClinicaGenotypeMolecular Sequence DataBiologymedicine.disease_causeGenomeFecesOpen Reading FramesPhylogeneticsVirologyPandemicGenotypemedicineHumansAmino Acid SequencePhylogenyCaliciviridae InfectionsRetrospective StudiesGeneticsnorovirus GII.4 variant New Orleans 2009 epidemiologyPhylogenetic treeNorovirusOutbreakNew OrleansVirologyGastroenteritisCaliciviridae InfectionsItalyNorovirusCapsid ProteinsSequence AlignmentThe Journal of general virology
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The membrane anchor of microsomal epoxide hydrolase from human, rat, and rabbit displays an unexpected membrane topology.

1997

The microsomal epoxide hydrolase (mEH) and cytochrome P450s catalyze the sequential formation of carcinogenic metabolites. According to one algorithm for predicting the membrane topology of proteins, the human, the rabbit, and the rat mEH should adopt a type II topology. The type II topology is also predicted by a recently established neuronal network which is trained to recognize signal peptides with very high accuracy. In contrast to these predictions we find, based on N-glycosylation analysis in a cell-free and in a cellular system, that the membrane anchor of human, rat, and rabbit mEH displays a type I topology. This result is correctly predicted by the positive inside rule in which ne…

Signal peptide1303 BiochemistryGlycosylationGlycosylationCytochromeStereochemistryRecombinant Fusion ProteinsImmunoblottingMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthProtein Sorting SignalsTransfectionBiochemistry1307 Cell BiologyCell membranechemistry.chemical_compoundSpecies Specificity1312 Molecular BiologymedicineElectrochemistryAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequenceEpoxide HydrolasesbiologyCell MembraneCell BiologyRatsmedicine.anatomical_structurechemistryMutagenesisMicrosomal epoxide hydrolaseMembrane topologyEpoxide HydrolasesCOS Cellsbiology.protein570 Life sciences; biologyRabbits1304 BiophysicsBiochemical and biophysical research communications
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The microsomal epoxide hydrolase has a single membrane signal anchor sequence which is dispensable for the catalytic activity of this protein

1994

The microsomal epoxide hydrolase (mEH) catalyses the hydrolysis of reactive epoxides which are formed by the action of cytochromes P-450 from xenobiotics. In addition it has been suggested that mEH might mediate the transport of bile acids. For the mEH it has been shown that it is co-translationally inserted into the endoplasmic reticulum. Here we demonstrate that the N-terminal 20 amino acid residues of this protein serve as its single membrane anchor signal sequence and that the function of this sequence can also be supplied by a cytochrome P-450 (CYP2B1) anchor signal sequence. The evidence supporting this conclusion is as follows: (i) the rat mEH and a CYP2B1-mEH fusion protein, in whic…

Signal peptideDNA ComplementaryCytochromeMolecular Sequence DataProtein Sorting SignalsBiochemistryCatalysisDogsMicrosomesAnimalsAmino Acid SequenceEpoxide hydrolasePancreasMolecular BiologyEpoxide HydrolasesBase SequenceCell-Free SystembiologyChemistryEndoplasmic reticulumCell MembraneTemplates GeneticCell BiologyFusion proteinRatsMembraneBiochemistryProtein BiosynthesisMicrosomal epoxide hydrolaseMicrosomebiology.proteinResearch ArticleBiochemical Journal
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dfh is a Drosophila homolog of the Friedreich's ataxia disease gene

2000

Abstract A putative Drosophila homolog of the Friedreich's ataxia disease gene (FRDA) has been cloned and characterized; it has been named Drosophila frataxin homolog (dfh). It is located at 8C/D position on X chromosome and is spread over 1 kb, a much smaller genomic region than the human gene. Its genomic organization is simple, with a single intron dividing the coding region into two exons. The predicted encoded product has 190 amino acids, being considered a frataxin-like protein on the basis of the sequence and secondary structure conservation when compared with human frataxin and related proteins from other eukaryotes. The closest match between the Drosophila and the human proteins in…

Signal peptideDNA ComplementaryEmbryo NonmammalianMolecular Sequence DataMutantEmbryonic DevelopmentGenes InsectExonIron-Binding ProteinsGeneticsAnimalsDrosophila ProteinsCoding regionAmino Acid SequenceRNA MessengerCloning MolecularGeneIn Situ HybridizationGenomic organizationGeneticsSequence Homology Amino AcidbiologyIntronGene Expression Regulation DevelopmentalDNAExonsSequence Analysis DNAGeneral MedicineBlotting NorthernIntronsPhosphotransferases (Alcohol Group Acceptor)Drosophila melanogasterFriedreich AtaxiaFrataxinbiology.proteinDrosophilaSequence AlignmentGene
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Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor.

1998

A 4-kb DNA segment of Tenebrio molitor (Insecta, Coleoptera) genomic DNA containing two larval-pupal cuticular genes has been cloned and sequenced. These genes, transcribed in opposite directions, are related in DNA sequence and the proteins encoded are very similar. Each of them contains a single intron located inside the sequence encoding the signal peptide, and a conserved sequence at -200 bp from the mRNA start position. These similarities in sequence suggest that these genes have evolved by duplication followed by diversification and that they are members of a family of genes with a common ancestry. They are the first example of clustered genes in Tenebrio molitor.

Signal peptideDNA ComplementaryMolecular Sequence DataGenes InsectBiologyBiochemistryDNA sequencingConserved sequenceEvolution MolecularGene duplicationAnimalsAmino Acid SequenceTenebrioPeptide sequenceGeneIn Situ HybridizationGeneticsBase SequenceSequence Homology Amino AcidfungiIntronMetamorphosis BiologicalGene Expression Regulation DevelopmentalIntronsgenomic DNAMultigene FamilyInsect ProteinsEuropean journal of biochemistry
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