Search results for " Homology"

showing 10 items of 633 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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Kontsevich–Zagier Periods

2017

We compare the set of Kontsevich–Zagier periods defined by integrals over semi-algebraic subsets of \(\mathbb {R}^n\) with cohomological periods.

Set (abstract data type)CombinatoricsMathematics::K-Theory and HomologyMathematics::Quantum AlgebraMathematics::Number TheoryImaginary numberMathematics
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Hochschild Cohomology Theories in White Noise Analysis

2008

We show that the continuous Hochschild cohomology and the differential Hochschild cohomology of the Hida test algebra endowed with the normalized Wick product are the same.

Sheaf cohomologyPure mathematicswhite noise analysisGroup cohomologyMathematics::Number TheoryFOS: Physical sciencesMathematics::Algebraic TopologyHochschild cohomologyGeneral Relativity and Quantum CosmologyCup productMathematics::K-Theory and HomologyMathematics::Quantum AlgebraMathematics - Quantum AlgebraFOS: MathematicsDe Rham cohomologyQuantum Algebra (math.QA)Equivariant cohomologyWick productČech cohomologyMathematical PhysicsMathematicslcsh:MathematicsMathematical Physics (math-ph)lcsh:QA1-939CohomologyGeometry and TopologyAnalysis
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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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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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Molecular cloning and primary structure of a Rhesus (Rh)-like protein from the marine sponge Geodia cydonium

1997

In humans, the 30,000 M(r) Rhesus (Rh) polypeptide D (RhD) is a dominant antigen (Ag) of the Rh blood group system. To date, an Rh-like protein has been found in chimpanzees, gorillas, gibbons, and rhesus monkeys. Related to the 30,000 M(r) Rh Ag protein are two polypeptides of 50,000 M(r), the human 50,000 M(r) Rh Ag and the RhD-like protein from Caenorhabditis elegans. The function of all these proteins is not sufficiently known. Here we characterize a cDNA clone (GCRH) encoding a putative 57,000 M(r) polypeptide from the marine sponge Geodia cydonium, which shares sequence similarity both to the RhD Ag and the Rh50 glycoprotein. The sponge Rh-like protein comprises 523 aa residues; hydro…

Signal peptideDNA ComplementaryMolecular Sequence DataImmunologyMolecular cloningGeneticsAnimalsHumansAmino Acid SequenceCloning MolecularCaenorhabditis elegansGlycoproteinschemistry.chemical_classificationRh-Hr Blood-Group SystemBase SequenceSequence Homology Amino AcidbiologyProtein primary structurebiology.organism_classificationMolecular biologyPoriferaSpongeTransmembrane domainchemistryGlycoproteinRh blood group systemImmunogenetics
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Complete sequence, expression and evolution of two members of the hexamerin protein family during the larval development of the rice moth, Corcyra ce…

2002

Three distinct types of storage hexamerins are expressed in the "last-instar" larvae of the rice moth, Corcyra cephalonica. A cDNA expression library was constructed from fat body-RNA and screened with a polyclonal antibody raised against purified hexamerin (SP2) of Corcyra cephalonica. Two slightly different "full-length" hexamerin cDNA clones (Hex2a and Hex2b) were isolated and sequenced. Both include open reading frames of 2109 bp which are translated into polypeptides of 703 amino acids with 92.5% identity. Signal peptides of 19 amino acids are present at the N-termini. The 684 amino acids native proteins have a high content of aryl groups (17.6%). According to both the criteria for ami…

Signal peptideDNA ComplementaryProtein familyBlotting WesternMolecular Sequence DataMothsBiochemistryEvolution MolecularComplete sequenceComplementary DNAEscherichia coliAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino AcidbiologyfungiBlotting Northernbiology.organism_classificationRecombinant ProteinsAmino acidOpen reading framechemistryBiochemistryRice mothLarvaInsect ScienceInsect ProteinsInsect Biochemistry and Molecular Biology
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mp23, a Theileria parva transmembrane protein with homology to the protein disulfide isomerase family

2002

The protozoan parasite Theileria parva (Apicomplexa) causes the bovine disease East Coast Fever in endemic areas in Subsaharan Africa. The intralymphocytic schizont stage is largely responsible for the pathogenicity and induces a transformed phenotype in host cells [1]. Current evidence supports a model in which the schizont perturbs the immune response by inducing production of cytokines and stimulating the growth of parasitized cells [2]. We were interested to identify parasite proteins involved in parasite/host interaction and have described earlier a screening procedure for identification of schizont stage-exported proteins based on cell-free expression of cDNA and testing for transloca…

Signal peptideDNA ComplementarySequence Homology Amino AcidcDNA libraryEndoplasmic reticulumTheileria parvaMolecular Sequence DataProtein Disulfide-IsomerasesProtozoan ProteinsMembrane ProteinsSequence Analysis DNABiologyTheileria parvabiology.organism_classificationMolecular biologyTransmembrane proteinMembrane proteinComplementary DNAparasitic diseasesAnimalsParasitologyAmino Acid SequenceProtein disulfide-isomeraseMolecular BiologyMolecular and Biochemical Parasitology
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Diplopod hemocyanin sequence and the phylogenetic position of the Myriapoda

2001

Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two distinct subunits that are arranged in a 6 x 6 native molecule. The cloned hemocyanin subunit cDNA codes of for a polypeptide of 653 amino acids (75.5 kDa) that includes a signal peptide of 18 amino acids. The sequence closely resembles that of the chelicerate hemocyanins. Molecular phylogenetic analyses reject with high statistical con…

Signal peptideDNA Complementarymedicine.medical_treatmentMolecular Sequence DataMyriapodachemical and pharmacologic phenomenaBiologycomplex mixturesEvolution MolecularSequence Analysis ProteinGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyArthropodsEcology Evolution Behavior and SystematicsPhylogenyPhylogenetic treeSequence Homology Amino Acidhemic and immune systemsHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationSpirostreptusSister groupEvolutionary biologyHemocyaninsChelicerataSequence AlignmentSpirostreptidae
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The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family

1992

This study was initiated to gain further insight into the structural features of the mammalian fetuin family. The cDNA structures of sheep and pig fetuin were determined. The cDNA insert encoding sheep (pig) fetuin comprised 1550 (1470) nucleotides, including 54 (46) nucleotides encoding a signal peptide of 18 (15) residues and 1038 (1041) nucleotides encoding the 346 (347) amino acids of the mature plasma protein. The predicted amino-terminal sequence of the mature pig fetuin was confirmed by the amino-terminal sequence of the purified protein. However, two alternative sheep amino-terminal sequences were found in fetuin purified from the plasma of a single sheep fetus; the minor product wa…

Signal peptideGlycosylationSwineBlotting WesternMolecular Sequence DataSequence alignmentBiologyBiochemistrySequence Homology Nucleic AcidComplementary DNAEndopeptidasesAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceMammalschemistry.chemical_classificationSheepBase SequenceSerine EndopeptidasesStructural geneNucleic acid sequenceMembrane ProteinsDNAMolecular biologyFetuinAmino acidBiochemistrychemistryElectrophoresis Polyacrylamide Gelalpha-FetoproteinsEuropean Journal of Biochemistry
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