Search results for "Chickens"

showing 10 items of 147 documents

The purification and properties of nucleoside phosphotransferase from mucosa of chicken intestine

1984

Abstract (1) Nucleoside phosphotransferase (nucleotide:3′-deoxynucleoside 5′-phosphotransferase, EC 2.7.1.77) has been purified from chicken intestine mucosa to apparent homogeneity. The enzyme is represented by a multisubunit protein at different degrees of association. It can dissociate into a compoenent with a marked fall in catalytic activity. (2) The associated forms are similar to the enzyme previously purified from chick embryo as regards: substrate specificity both with respect to nucleoside monophosphate donors and to deoxyribonucleoside acceptors; sigmoidicity in the rate curve with a variable phosphate donor; instability to heat, dilution and lowering of pH; the activating and pr…

StereochemistryCations DivalentProtein subunitBiophysicsBiologyBiochemistrychemistry.chemical_compoundStructural BiologySettore BIO/10 - BiochimicaNucleoside phosphotransferaseCentrifugation Density GradientAnimalsUreaNucleotideEnzyme kineticsIntestinal MucosaMolecular Biologychemistry.chemical_classificationNucleotidesPhosphotransferasesPhosphatenucleoside phosphotransferaseDeoxyuridineDeoxyribonucleosideMolecular WeightKineticsEnzymechemistryBiochemistryAlcoholsChromatography GelElectrophoresis Polyacrylamide GelChickens
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Eukaryotic tRNAs(Pro): primary structure of the anticodon loop; presence of 5-carbamoylmethyluridine or inosine as the first nucleoside of the antico…

1990

The modified nucleoside U*, located in the first position of the anticodon of yeast, chicken liver and bovine liver tRNA(Pro) (anticodon U*GG), has been determined by means of TLC, HPLC, ultraviolet spectrum and gas chromatography-mass spectrometry. The structure was established as 5-carbamoylmethyluridine (ncm5U). In addition, we report on the primary structures of the above-mentioned tRNAs as well as those which have the IGG anticodon. In yeast, the two tRNA(Pro) (anticodons U*GG and IGG) differ by eight nucleotides, whereas in chicken and in bovine liver, both anticodons are carried by the same 'body tRNA' with one posttranscriptional exception at position 32, where pseudouridine is asso…

StereochemistryMolecular Sequence DataBiophysicsBiologyBiochemistryPseudouridinechemistry.chemical_compoundRNA Transfer ProRNA TransferStructural BiologyYeastsGeneticsmedicineAnticodonAnimalsNucleotideInosineUridinechemistry.chemical_classificationChromatographyBase SequenceMolecular StructureProtein primary structureFungal geneticsRNARNA FungalRNA Transfer Amino Acid-SpecificInosinechemistryBiochemistryTransfer RNANucleic Acid ConformationCattleSpectrophotometry UltravioletNucleosideChickensmedicine.drugBiochimica et biophysica acta
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High-resolution crystal structure of an avidin-related protein: insight into high-affinity biotin binding and protein stability.

2004

The chicken avidin gene belongs to an extended gene family encoding seven avidin-related genes (AVRs), of which only avidin is expressed in the chicken. The sequences of AVR4 and AVR5 are identical and the common protein (AVR4) has been expressed both in insect and bacterial systems. The recombinant proteins are similarly hyperthermostable and bind biotin with similarly high affinities. AVR4 was crystallized in the apo and biotin-complexed forms and their structures were determined at high resolution. Its tertiary and quaternary structures are very similar to those of avidin and streptavidin. Its biotin-binding site shows only a few alterations compared with those of avidin and streptavidin…

StreptavidinBiotin bindingHot TemperatureBiotinBiologylaw.inventionchemistry.chemical_compoundBiotinStructural BiologylawAnimalsProtein Structure QuaternaryThermostabilityBacteriaHydrogen BondingGeneral MedicineAvidinAffinitiesBiochemistrychemistryBiotinylationData Interpretation StatisticalBiophysicsRecombinant DNAbiology.proteinStreptavidinCrystallizationBaculoviridaeChickensAvidinProtein BindingActa crystallographica. Section D, Biological crystallography
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Engineering of chicken avidin: a progressive series of reduced charge mutants.

1998

Avidin, a positively charged egg-white glycoprotein, is a widely used tool in biotechnological applications because of its ability to bind biotin strongly. The high pI of avidin (approximately 10.5), however, is a hindrance in certain applications due to non-specific (charge-related) binding. Here we report a construction of a series of avidin charge mutants with pIs ranging from 9.4 to 4.7. Rational design of the avidin mutants was based on known crystallographic data together with comparative sequence alignment of avidin, streptavidin and a set of avidin-related genes which occur in the chicken genome. All charge mutants retained the ability to bind biotin tightly according to optical bio…

StreptavidinDNA ComplementaryHot TemperatureMutantBiophysicsBiotinSequence alignmentBiologySpodopteraProtein EngineeringBiochemistrychemistry.chemical_compoundstomatognathic systemBiotinStructural BiologyGeneticsAnimalsMolecular BiologyCharge mutantAvidin-biotin technologyRational designCell BiologyProtein engineeringrespiratory systemAvidinDNA-Binding ProteinschemistryBiochemistryBiotinylationbiology.proteinMutagenesis Site-DirectedChickensAvidinFEBS letters
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Recombinant avidin and avidin-fusion proteins.

2000

Both chicken egg-white avidin and its bacterial relative streptavidin are well known for their extraordinary high affinity with biotin (Kd approximately 10(-15) M). They are widely used as tools in a number of affinity-based separations, in diagnostic assays and in a variety of other applications. These methods have collectively become known as (strept)avidin-biotin technology. Biotin can easily and effectively be attached to different molecules, termed binders and probes, without destroying their biological activity. The exceptional stability of the avidin-biotin complex and the wide range of commercially available reagents explain the popularity of this system. In order by genetic enginee…

StreptavidinInsectaAffinity labelRecombinant Fusion ProteinsBiotinBioengineeringProtein Engineeringlaw.inventionchemistry.chemical_compoundstomatognathic systemBiotinlawEscherichia coliAnimalsMolecular BiologybiologyCell MembraneAffinity LabelsProtein engineeringrespiratory systemAvidinFusion proteinRecombinant ProteinschemistryBiochemistryBiotinylationRecombinant DNAbiology.proteinBaculoviridaeChickensBiotechnologyAvidinBiomolecular engineering
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Dimer-tetramer transition between solution and crystalline states of streptavidin and avidin mutants.

2003

ABSTRACT The biotin-binding tetrameric proteins, streptavidin from Streptomyces avidinii and chicken egg white avidin, are excellent models for the study of subunit-subunit interactions of a multimeric protein. Efforts are thus being made to prepare mutated forms of streptavidin and avidin, which would form monomers or dimers, in order to examine their effect on quaternary structure and assembly. In the present communication, we compared the crystal structures of binding site W→K mutations in streptavidin and avidin. In solution, both mutant proteins are known to form dimers, but upon crystallization, both formed tetramers with the same parameters as the native proteins. All of the intersub…

StreptavidinModels MolecularStereochemistryProtein ConformationDimerBiotinCrystallography X-RayMicrobiologychemistry.chemical_compoundProtein structureBiotinTetramerEgg WhiteStructural BiologyAnimalsProtein Structure QuaternaryMolecular BiologyBinding SitesbiologyAvidinStreptomycesSolutionschemistryBiochemistryBiotinylationMutationbiology.proteinProtein quaternary structureStreptavidinCarrier ProteinsCrystallizationChickensDimerizationAvidinJournal of bacteriology
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Molecular cloning and nucleotide sequence of chicken avidin-related genes 1-5.

1994

Using avidin cDNA as a hybridisation probe, we detected a gene family whose putative products are related to the chicken egg-white avidin. Two overlapping genomic clones were found to contain five genes (avidin-related genes 1–5, avrl-avr5), which have been cloned, characterized and sequenced. All of the genes have a four-exon structure with an overall identity with the avidin cDNA of 88–92%. The genes appear to have no pseudogenic features and, in fact, two of these genes have been shown to be transcribed. The putative proteins share a sequence identity of 68–78% with avidin. The amino acid residues responsible for the biotin-binding activity of avidin and the bacterial biotin-binding prot…

StreptavidinTranscription GeneticMolecular Sequence DataRestriction MappingBiotinBiologyMolecular cloningBiochemistryPolymerase Chain Reactionchemistry.chemical_compoundstomatognathic systemBacterial ProteinsIn vivoComplementary DNASequence Homology Nucleic AcidAnimalsAmino Acid SequenceCloning MolecularProtein PrecursorsGeneConserved SequenceRegulation of gene expressionGeneticsSequence Homology Amino AcidNucleic acid sequenceDNAExonsAvidinRecombinant Proteinschemistrybiology.proteinStreptavidinChickensPseudogenesAvidinEuropean journal of biochemistry
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A Transition Zone Complex Regulates Mammalian Ciliogenesis and Ciliary Membrane Composition

2011

Mutations in genes encoding ciliary components cause ciliopathies, but how many of these mutations disrupt ciliary function is unclear. We investigated Tectonic1 (Tctn1), a regulator of mouse Hedgehog signaling, and found that it is essential for ciliogenesis in some, but not all, tissues. Cell types that do not require Tctn1 for ciliogenesis require it to localize select membrane-associated proteins to the cilium, including Arl13b, AC3, Smoothened and Pkd2. Tctn1 forms a complex with multiple ciliopathy proteins associated with Meckel (MKS) and Joubert (JBTS) syndromes, including Mks1, Tmem216, Tmem67, Cep290, B9d1, Tctn2, and Cc2d2a. Components of the Tectonic ciliopathy complex colocaliz…

TMEM67Inbred C57BLCiliopathiesMedical and Health SciencesMice0302 clinical medicineCerebellumMorphogenesisEye AbnormalitiesEncephalocelePediatricMice Knockout0303 health sciencesPolycystic Kidney DiseasesCiliumCiliary transition zoneBiological SciencesKidney Diseases CysticCell biologyOrgan SpecificityCiliary Motility DisordersKidney DiseasesRabbitsAbnormalitiesMultipleRetinitis PigmentosaCiliary Motility DisordersSignal TransductionKnockoutBiologyRetinaArticle03 medical and health sciencesCysticRare DiseasesCerebellar DiseasesCiliogenesisGeneticsMatrix-Assisted Laser Desorption-IonizationAnimalsHumansAbnormalities MultipleCiliaCiliary membrane030304 developmental biologySpectrometryCell MembraneMembrane ProteinsMassPeptide FragmentsMice Inbred C57BLSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCiliary baseChickens030217 neurology & neurosurgeryDevelopmental BiologyNature genetics
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Agouti-Related Proteins (AGRPs) and Agouti-Signaling Peptide (ASIP) in Fish and Chicken

2005

We performed an intensive search on sequence databases to identify orthologues of ASIP and AGRP peptides in a number of different species, revealing a number of genomic fragments coding for the C-terminal part of agouti-related motifs, different from annotated peptide sequences, including one fragment from chicken, two from zebrafish, two from Fugu (Takifugu rubripes), and three from Tetraodon (Tetraodon nigroviridis). We have thus shown for the first time that both AGRP and ASIP genes exist in many species in "lower vertebrates" and were most probably present in early stages of vertebrate evolution.

Takifugu rubripesMolecular Sequence DataTetraodon nigroviridisGeneral Biochemistry Genetics and Molecular BiologySpecies SpecificityHistory and Philosophy of Sciencebiology.animalDatabases GeneticAnimalsAgouti-Related ProteinAmino Acid SequenceTetraodonGeneZebrafishPeptide sequencePhylogenyGeneticsbiologyFuguGeneral Neurosciencedigestive oral and skin physiologyFishesProteinsVertebratebiology.organism_classificationAgouti Signaling ProteinIntercellular Signaling Peptides and ProteinsChickensAnnals of the New York Academy of Sciences
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Fat and salt contents affect the in-mouth temporal sodium release and saltiness perception of chicken sausages

2013

In cooked meats, sodium chloride is involved in taste, texture and flavour release. So a reduction in the salt content may have an impact on overall perception and acceptability. The aim of this study was to evaluate the influence of composition on sodium release and saltiness intensity in chicken sausages. The rheological properties of the sausages differed according to composition. Temporal sodium release and temporal saltiness intensity were evaluated by four selected subjects when eating sausages. At each time point, the effect of the salt level in sausages on sodium release was positive and highly significant. The effect of lipids on sodium release was negative. Concerning perception, …

TasteTime FactorsSalt contentSodiumFlavourchemistry.chemical_elementSalt (chemistry)Sodium ChlorideFood Preferences0404 agricultural biotechnologyAnimalsFood sciencePoultry ProductsComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationSodium0402 animal and dairy science04 agricultural and veterinary sciencesConsumer BehaviorDietary Fats040401 food science040201 dairy & animal sciencechemistryTasteComposition (visual arts)Chickens[SDV.AEN]Life Sciences [q-bio]/Food and NutritionFood Science
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