Search results for "Protein primary structure"

showing 10 items of 29 documents

Complete Hemocyanin Subunit Sequences of the Hunting SpiderCupiennius salei

2002

Hemocyanins are large copper-containing respiratory proteins found in many arthropod species. Scorpions and orthognath spiders possess a highly conserved 4 x 6-mer hemocyanin that consists of at least seven distinct subunit types (termed a to g). However, many "modern" entelegyne spiders such as Cupiennius salei differ from the standard arachnid scheme and have 2 x 6-mer hemocyanins. Here we report the complete primary structure of the 2 x 6-mer hemocyanin of C. salei as deduced from cDNA sequencing, gel electrophoresis, and matrix-assisted laser desorption spectroscopy. Six distinct subunit types (1 through 6) and three additional allelic sequences were identified. Each 1 x 6-mer half-mole…

ArachnidSpiderbiologyProtein subunitmedicine.medical_treatmentProtein primary structuremyrHemocyaninCell BiologyAnatomybiology.organism_classificationcomplex mixturesBiochemistryCupiennius saleiEvolutionary biologymedicineArthropodMolecular BiologyJournal of Biological Chemistry
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Molluscan Shell Proteins: Primary Structure, Origin, and Evolution

2007

In the last few years, the field of molluscan biomineralization has known a tremendous mutation, regarding fundamental concepts on biomineralization regulation as well as regarding the methods of investigation. The most recent advances deal more particularly with the structure of shell biominerals at nanoscale and the identification of an increasing number of shell matrix protein components. Although the matrix is quantitatively a minor constituent in the shell of mollusks (less than 5% w/w), it is, however, the major component that controls different aspects of the shell formation processes: synthesis of transient amorphous minerals and evolution to crystalline phases, choice of the calciu…

Calcite0303 health sciencesComponent (thermodynamics)AragoniteProtein primary structureShell (structure)02 engineering and technologyBiologyMatrix (biology)engineering.material021001 nanoscience & nanotechnology03 medical and health scienceschemistry.chemical_compoundCalcium carbonatechemistryChemical physicsengineering0210 nano-technology030304 developmental biologyBiomineralization
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Characterization and phylogenetic analysis of a cDNA encoding the Fes/FER related, non-receptor protein-tyrosine kinase in the marine sponge Sycon ra…

1998

Abstract In search of ancient versions of phylogenetically conserved genes/proteins, which are typical for multicellular animals, we have decided to analyse marine sponges (Porifera), the most ancient and most primitive metazoan organisms. We report here the complete nucleotide sequence of Sycon raphanus cDNA coding for a 879 aa long protein (100 kDa), which displays high overall similarity in primary structure and organization of domains with non-receptor tyrosine kinases (TKs) from the Fes/FER family. The encoded protein, which we named Fes/FER_SR, has a highly conserved, 260 aa long tyrosine kinase domain at the C-terminus. Amino-terminal to the catalytic domain is an 85 aa long SH2 doma…

DNA Complementaryanimal structuresMolecular Sequence DataBiologySH2 domainHomology (biology)PhylogeneticsProto-Oncogene ProteinsComplementary DNAGeneticsAnimalsAmino Acid SequenceSycon raphanusPhylogenyGeneticsSequence Homology Amino AcidProtein primary structureNucleic acid sequenceSequence Analysis DNAGeneral MedicineProtein-Tyrosine Kinasesbiology.organism_classificationPoriferaBiochemistryOncogenes; Signal transduction; SH2 domain; Metazoa; Porifera; PhylogenySequence AlignmentTyrosine kinaseGene
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A new metallothionein gene from the giant keyhole limpet Megathura crenulata.

2003

Abstract Metallothioneins (MTs) are small soluble proteins ubiquitously expressed in animals and plants. Different isoforms are present in deuterostomes and protostomes. They do not differ greatly in primary structure, but are clearly distinguishable. Here, I present the gene and the complete cDNA of a novel MT from the mollusk Megathura crenulata . This protein is closely related to the Cu-inducible MTs of the vineyard snail Helix pomatia , but has also some minor sequence features typical of Cd-inducible isoforms of H . pomatia and other molluscs. Overall, the deduced primary structure is similar to the known molluscan MTs, but in addition possesses an insertion of 5 amino acids not found…

Gene isoformDNA ComplementaryPhysiologyHealth Toxicology and MutagenesisMolecular Sequence DataSnailMegathura crenulataToxicologyBiochemistryPentapeptide repeatPolymerase Chain ReactionSpecies Specificitybiology.animalComplementary DNAMetallothioneinAnimalsAmino Acid SequenceGenomebiologyBase SequenceSequence Homology Amino AcidProtein primary structureCell BiologyGeneral MedicineHelix pomatiaSequence Analysis DNAbiology.organism_classificationMolecular biologyBiochemistryMolluscaMetallothioneinCarrier ProteinsComparative biochemistry and physiology. Toxicologypharmacology : CBP
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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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Nucleotide sequence of the 18S rDNA from the microalgaNanochlorum eucaryotum

1988

GeneticsBase SequenceMolecular Sequence DataNucleic acid sequenceProtein primary structureEukaryotaNanochlorum eucaryotumBiologyRibosomal RNADNA Ribosomal18S ribosomal RNAlaw.inventionRNA RibosomallawRNA Ribosomal 18SGeneticsRecombinant DNAGeneRibosomal DNANucleic Acids Research
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The Primary Structure of Several Hemoglobin Genes from the Genome of Chironomus tentans

1991

In addition to Chironomus thummi thummi, Chironomus tentans is another Chironomid species in which the Hb proteins have been investigated (1) and in which the Hb genes have been localized (2). Thus, this species is an ideal candidate for the study of Hb gene structure and evolution.

GeneticsProtein primary structureChironomus thummiHemoglobinBiologyGenomeGeneChironomus tentans
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The primary structure of cytoplasmic initiator tRNAMetfromSchizosaccharomyces pombe

1993

GeneticsRNA Transfer MetBase SequencebiologyMolecular Sequence DataProtein primary structureNucleic acid sequenceRNARNA Fungalbiology.organism_classificationEukaryotic translationBiochemistryCytoplasmSchizosaccharomycesTransfer RNASchizosaccharomyces pombeGeneticsSchizosaccharomycesNucleic Acids Research
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Tracing keratin evolution: catalog, expression patterns and primary structure of shark (Scyliorhinus stellaris) keratins.

1998

We have studied individual keratins of an elasmobranch, the shark Scyliorhinus stellaris (the lesser-spotted dogfish). From various shark tissues, notably skin and stomach, cytoskeletal proteins were isolated and then separated by two-dimensional polyacrylamide gel electrophoresis. Using complementary keratin blot-binding assays and immunoblotting, among these proteins we identified a variety of type I and type II keratins. According to their tissue-specific expression, we distinguished Is and IIs keratins from IE and IIE keratins ("S" and "E" from "simple epithelial" and "epidermal", respectively). Guinea pig antibodies which in immunoblots specifically labeled the entire range of identifi…

HistologyDNA ComplementaryMolecular Sequence Datamacromolecular substancesPathology and Forensic MedicineKeratinAnimalsHumansAmino Acid SequenceIntermediate filamentPolyacrylamide gel electrophoresisPeptide sequencechemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyBase SequenceProtein primary structureCell BiologyGeneral MedicineKeratin 6Abiology.organism_classificationMolecular biologyBiological EvolutionchemistryMicroscopy FluorescenceSharksKeratinshuman activitiesScyliorhinus stellarisEuropean journal of cell biology
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Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: Sequence, expression patterns and in vitro assembly

2002

In the shark Scyliorhinus stellaris we have biochemically identified and cDNA-cloned orthologs of human vimentin and desmin, SstV and SstD, as deduced from immunoblotting and sequence alignment with teleost, frog and human vimentin and desmin, respectively. This allowed us to further clarify the relationship of previously identified lower vertebrate intermediate filament proteins to mammalian vimentin and desmin. Immunofluorescence microscopy with antibodies H5 and VIM13.2 showed vimentin expression in shark eye and brain and absence in epithelia, which resembles the situation in higher vertebrates. In addition, SstV is expressed in many mesenchymal cell types which corresponds to the case …

HistologyNeurofilamentMolecular Sequence DataIntermediate FilamentsGene ExpressionVimentinmacromolecular substancesDesminPathology and Forensic MedicineEvolution MolecularProtein filamentKeratinAnimalsVimentinIntermediate filamentPhylogenychemistry.chemical_classificationSequence Homology Amino AcidbiologyProtein primary structureCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyMicroscopy ElectronchemistrySharksbiology.proteinDesminScyliorhinus stellarisEuropean Journal of Cell Biology
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