Search results for "Protein Subunit"

showing 10 items of 243 documents

Isolation and partial characterization of a cytochrome-o complex from chromatophores of the photosynthetic bacterium Rhodospirillum rubrum FR1.

1989

A cytochrome-o complex was isolated from chromatophores of photoheterotrophically grown Rhodospirillum rubrum FR1. The enzyme was extracted with the non-denaturating detergent taurodeoxycholate and subsequently purified by sucrose-density-gradient centrifugation and gel-permeation HPLC. The complex contains two types of cytochromes, one of them cytochrome o, and two copper atoms. It catalyzes the reduction of molecular oxygen, when N,N,N',N'-tetramethyl-p-phenylenediamine or ubiquinol 10 are offered as electron donors. The oxidase activity is inhibited by cyanide, carbon monoxide and 2-heptyl-2-hydroxyquinoline N-oxide. The molecular mass of the protein is 136 +/- 15 kDa. The subunit analys…

Gel electrophoresisOxidase testUbiquinolHemeproteinCytochromebiologyMolecular massChemistryProtein subunitEscherichia coli ProteinsRhodospirillum rubrumPhotosynthetic Reaction Center Complex ProteinsDithioniteBacterial Chromatophoresbiology.organism_classificationCytochrome b GroupBiochemistrychemistry.chemical_compoundBiochemistryBacterial Proteinsbiology.proteinCytochromesElectrophoresis Polyacrylamide GelRhodospirillumEuropean journal of biochemistry
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Gene structure and hemocyanin isoform HtH2 from the mollusc Haliotis tuberculata indicate early and late intron hot spots.

2002

Abstract We have cloned and sequenced cDNAs coding for the complete primary structure of HtH2, the second hemocyanin isoform of the marine gastropod Haliotis tuberculata. The deduced protein sequence comprises 3399 amino acids, corresponding to a molecular mass of 392 kDa. It shares only 66% of structural identity with the previously analysed first isoform HtH1, and according to a molecular clock, the two isoforms of Haliotis hemocyanin separated ca. 320 million years ago. By genomic polymerase chain reaction and 5′ race, we have also sequenced the complete gene of HtH2 (18,598 bp), except of the 5′ region in front of the secreted protein. It encompasses 15 exons and 14 introns and shows se…

Gene isoformDNA ComplementaryTime Factorsmedicine.medical_treatmentProtein subunitMolecular Sequence DataBiologyEvolution MolecularExonProtein sequencingGeneticsmedicineAnimalsProtein IsoformsAmino Acid SequenceGeneGeneticsBase SequenceSequence Homology Amino AcidProtein primary structureIntronHemocyaninGeneral MedicineDNAExonsSequence Analysis DNAIntronsGenesMolluscaHemocyaninsSequence AlignmentGene
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The diversity of GABAA receptors. Pharmacological and electrophysiological properties of GABAA channel subtypes.

1998

The amino acid gamma-aminobutyric-acid (GABA) prevails in the CNS as an inhibitory neurotransmitter that mediates most of its effects through fast GABA-gated Cl(-)-channels (GABAAR). Molecular biology uncovered the complex subunit architecture of this receptor channel, in which a pentameric assembly derived from five of at least 17 mammalian subunits, grouped in the six classes alpha, beta, gamma, delta, sigma and epsilon, permits a vast number of putative receptor isoforms. The subunit composition of a particular receptor determines the specific effects of allosterical modulators of the GABAARs like benzodiazepines (BZs), barbiturates, steroids, some convulsants, polyvalent cations, and et…

Gene isoformMacromolecular SubstancesProtein ConformationProtein subunitNeuroscience (miscellaneous)LoreclezoleConvulsantsBiologyInhibitory postsynaptic potentialGABAA-rho receptorSubstrate SpecificityGABA AntagonistsCellular and Molecular NeuroscienceBenzodiazepinesMiceChloride ChannelsmedicineAnimalsHumansProtein IsoformsReceptorGABA Agonistsgamma-Aminobutyric AcidAnestheticsMice KnockoutBinding SitesIon TransportGABAA receptorReceptors GABA-ARecombinant ProteinsRatsElectrophysiologyNeurologyBiochemistryBarbituratesSteroidsHeterologous expressionIon Channel Gatingmedicine.drugMolecular neurobiology
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Hemocyanin subunit organization of the gastropod Rapana thomasiana

1999

Abstract RtH1 and RtH2, the two hemocyanin isoforms of the prosobranch gastropod Rapana thomasiana, have been purified by anion-exchange chromatography and studied by SDS–PAGE and immunoelectrophoresis. Both subunit types are built up of eight functional units (FUs). Under reducing conditions subunit RtH2 splits into two fragments, RtH2- a – f and RtH2- gh, suggesting the presence of a disulfide bridge between FU2- f and FU2- g. By proteolytic cleavage of the subunits into three-, two-, and single-FU fragments, purification of fragments by HPLC, N-terminal sequencing of the peptides, and crossed-line immunoelectrophoresis, FUs- a – h of RtH2 and FU- a, FU- d, FU- e, and FU- f of RtH1 were i…

Gene isoformSubunitProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiophysicsImmunoelectrophoresisBiologyMegathura crenulataCleavage (embryo)BiochemistryHigh-performance liquid chromatographyHemocyaninRapana thomasianamedicineAnimalsProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyGasteropodsmedicine.diagnostic_testPancreatic ElastaseImmunochemistryStructureHemocyaninbiology.organism_classificationMolecular biologyPeptide FragmentsMolluscaHemocyanin; Gasteropods; Structure; SubunitHemocyaninsImmunoelectrophoresis Two-Dimensional
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Association of Whirlin with Cav1.3 (α1D) Channels in Photoreceptors, Defining a Novel Member of the Usher Protein Network

2010

Contains fulltext : 88383.pdf (Publisher’s version ) (Closed access) PURPOSE: Usher syndrome is the most common form of hereditary deaf-blindness. It is both clinically and genetically heterogeneous. The USH2D protein whirlin interacts via its PDZ domains with other Usher-associated proteins containing a C-terminal type I PDZ-binding motif. These proteins co-localize with whirlin at the region of the connecting cilium and at the synapse of photoreceptor cells. This study was undertaken to identify novel, Usher syndrome-associated, interacting partners of whirlin and thereby obtain more insights into the function of whirlin. METHODS: The database of ciliary proteins was searched for proteins…

Genetics and epigenetic pathways of disease [NCMLS 6]Calcium Channels L-TypeUsher syndromeProtein subunitImmunoelectron microscopyBlotting WesternPDZ domainRetinaCav1.3MiceTwo-Hybrid System TechniquesChlorocebus aethiopsmedicineAnimalsInner earRNA MessengerRats WistarDatabases ProteinMicroscopy ImmunoelectronPhotoreceptor Connecting CiliumIn Situ HybridizationRenal disorder [IGMD 9]RetinaVoltage-dependent calcium channelbiologyComputational BiologyMembrane Proteinsmedicine.diseaseeye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureCOS Cellsbiology.proteinsense organsFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateInvestigative Opthalmology & Visual Science
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Human complement C81 (C8 A) polymorphism: detection and segregation of new variants

1993

In addition to the earlier detected C81(A) rare variants A1, A2 (now A3) and B1 (now B2), six new rare variants (C81 A2 new, A4, A5, A6, M1 and B1new) are described within the polymorphism of the eighth component of human complement (alpha-gamma chain subunit). Except for A3, all rare C81 A variants are only detected by isoelectric focusing, and not by SDS polyacrylamide gel electrophoresis (PAGE), in the alpha-gamma subunit. In one individual out of approximately 700 individuals studied, a reversed position of the common allele (B vs A) was observed by SDS PAGE and the isofocusing technique. The segregation of A1, A3 and A4 could be followed in putative father/child combinations.

GeneticsComplement (group theory)Polymorphism GeneticIsoelectric focusingProtein subunitBiologyComplement C8Molecular biologyAllotypeHuman geneticsPolymorphism (computer science)GeneticsHumansElectrophoresis Polyacrylamide GelIsoelectric FocusingAllelePolyacrylamide gel electrophoresisAllelesGenetics (clinical)Human Genetics
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Native-state pea albumin and globulin behavior upon transglutaminase treatment

2015

International audience; The behavior of pea albumin (Alb) and globulin (Glob) in their native state upon microbial transglutaminase (MTGase) treatment was studied. Only Glob was able to form a gel, at up to a 10% (w/w) concentration, with a minimum gelling concentration of 6% (w/w), and with a cross-linking degree of 25%. The most affected Glob subunits were convicilin (71 kDa), vicilins (55, 50, and 35 kDa), and legumin acidic subunit (40 kDa). In contrast, the legumin basic subunit (20 kDa) and vicilins of molecular weight less than 20 kDa remained mostly intact in all studied conditions. The cross-linking degree of Alb was 12%, which was not sufficient to form MTGase-induced gel. Major a…

GlobulinTissue transglutaminaseProtein subunitBioengineering01 natural sciencesApplied Microbiology and BiotechnologyBiochemistry0404 agricultural biotechnologyNative stateLeguminPea albuminsDenaturation (biochemistry)[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCross-linking degreebiologyChemistry010401 analytical chemistryAlbuminglob (programming)04 agricultural and veterinary sciences040401 food scienceOptimum parameters0104 chemical sciencesBiochemistryPea globulinsbiology.proteinMicrobial transglutaminase properties
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Mosaic particles formed by wild-type hepatitis B virus core protein and its deletion variants consist of both homo- and heterodimers.

2003

AbstractCo-expression in Escherichia coli of wild-type (wt) hepatitis B virus core protein (HBc) and its naturally occurring variants with deletions at amino acid positions 77–93 or 86–93 leads to formation of mosaic particles, which consist of three dimer subunit compositions. These compositions are wt/variant HBc heterodimers and two types of homodimers, formed by wt HBc or the variant HBc themselves. Mosaic particles were found also when both HBc deletion variants 77–93 and 86–93 were co-expressed in E. coli. These findings are discussed in terms of their significance for hepatitis B virus pathogenesis and prospective use of mosaic particles in vaccine development.

Hepatitis B virusvirusesProtein subunitDimerBiophysicsExpressionPlasma protein bindingBiologymedicine.disease_causeMosaic particlesBiochemistrychemistry.chemical_compoundHepatitis B virus core proteinProtein structureStructural Biologyparasitic diseasesGeneticsmedicineHepatitis B VaccinesCloning MolecularProtein Structure QuaternaryMolecular BiologyEscherichia coliSequence Deletionchemistry.chemical_classificationHepatitis B virusViral Core ProteinsWild typevirus diseasesGenetic VariationCell BiologyHepatitis BDimer formationVirologyMolecular biologydigestive system diseasesAmino acidProtein SubunitschemistryDimerizationProtein BindingFEBS letters
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Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide

2011

DAPIT (Diabetes Associated Protein in Insulin-sensitive Tissues) is a small, phylogenetically conserved, 58 amino acid peptide that was previously shown to be down-regulated at mRNA level in insulin-sensitive tissues of type 1 diabetes rats. In this study we characterize a custom made antibody against DAPIT and confirm the mitochondrial presence of DAPIT on cellular level. We also show that DAPIT is localized in lysosomes of HUVEC and HEK 293T cells. In addition, we describe the histological expression of DAPIT in several tissues of rat and man and show that it is highly expressed especially in cells with high aerobic metabolism and epithelial cells related to active transport of nutrients …

HistologyCellular respirationProtein subunitBiophysicsPeptideV-ATPaseBiologyMitochondrionAntibodiesMitochondrial ProteinsHuman Umbilical Vein Endothelial CellsV-ATPaseAnimalsHumansmitochondrionta315lcsh:QH301-705.5PhylogenyDAPIT mitochondrion V-ATPase type 1 diabeteschemistry.chemical_classificationRegulation of gene expressionOriginal Papertype 1 diabetes.HEK 293 cellsMembrane ProteinsCell BiologyProton PumpsCell biologyMitochondriaRatsHEK293 CellsMembrane proteinchemistryBiochemistryGene Expression Regulationlcsh:Biology (General)Organ SpecificityLysosomesDAPITEuropean Journal of Histochemistry
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Cryptogein affects expression of alpha3, alpha6 and beta1 20S proteasome subunits encoding genes in tobacco.

2001

Twelve a and b 20S proteasome subunits cDNAs showing 70–82% identity with the corresponding genes in Arabidopsis or rice, and features of eukaryotic proteasome subunits were cloned in tobacco. Only b1-tcI 7, a3 and a6, 20S proteasome subunits encoding genes were up-regulated by cryptogein, a proteinaceous elicitor of plant defence reactions. These results led to the hypothesis that the activation of b1-tcI 7, a3 and a6 could induce a specific proteolysis involved in the hypersensitive response and systemic acquired resistance monitored by cryptogein. In eukaryotes, the 26S proteasome is the central multicatalytic proteinase complex comprising two subcomplexes: the 20S core particle that per…

Hypersensitive responseProteasome Endopeptidase ComplexPhysiologyProtein subunitProteolysisMolecular Sequence DataPlant ScienceGenes PlantGene Expression Regulation EnzymologicFungal ProteinsGene Expression Regulation PlantMultienzyme ComplexesArabidopsisGene expressionTobaccomedicineAmino Acid SequenceGenePlant Diseasesbiologymedicine.diagnostic_testAlgal Proteinsbiology.organism_classificationPlants Genetically ModifiedCysteine EndopeptidasesProteasomeBiochemistryProtein foldingJournal of experimental botany
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