Search results for "Disulfide bond"

showing 10 items of 17 documents

Maternal Inheritance of a Recessive RBP4 Defect in Canine Congenital Eye Disease

2018

SUMMARY Maternally skewed transmission of traits has been associated with genomic imprinting and oocyte-derived mRNA. We report canine congenital eye malformations, caused by an amino acid deletion (K12del) near the N terminus of retinol-binding protein (RBP4). The disease is only expressed when both dam and offspring are deletion homozygotes. RBP carries vitamin A (retinol) from hepatic stores to peripheral tissues, including the placenta and developing eye, where it is required to synthesize retinoic acid. Gestational vitamin A deficiency is a known risk factor for ocular birth defects. The K12del mutation disrupts RBP folding in vivo, decreasing its secretion from hepatocytes to serum. T…

0301 basic medicineMaleNon-Mendelian inheritanceProtein Foldingcongenital eye defectEye Diseasesgenetic structuresNATIVE DISULFIDE BONDSMedical PhysiologyRetinoic acidReproductive health and childbirth413 Veterinary scienceMicrophthalmiavitamin Achemistry.chemical_compoundPlasmaA-vitamiini2.1 Biological and endogenous factorsMicrophthalmosPrealbuminCRYSTAL-STRUCTUREAetiologyBase Pairinglcsh:QH301-705.5Sequence DeletionPediatricwhole genome sequencingVITAMIN-A-DEFICIENCYANOPHTHALMIAPenetrancePedigreemedicine.anatomical_structurePhenotypeFemalemedicine.medical_specialtyGenotypeENDOPLASMIC-RETICULUMGenes RecessiveMETABOLISMBiologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesDogscanine geneticsInternal medicinePlacentaRETINOL-BINDING-PROTEINGeneticsmedicineAnimalsHumansRecessiveMALFORMATIONSBIOCHEMICAL BASISAmino Acid SequenceAlleleEye Disease and Disorders of VisionNutritiongenome-wide association study030102 biochemistry & molecular biologywestern blottingMUTATIONSta1184RBP4maternal inheritancemedicine.diseaseRetinol-Binding ProteinsRetinol binding proteinnuclear magnetic resonance030104 developmental biologyEndocrinologychemistryGeneslcsh:Biology (General)microphthalmiaGenetic LociHela Cells1182 Biochemistry cell and molecular biologyCongenital Structural Anomalies3111 BiomedicineBiochemistry and Cell BiologyDigestive DiseasesGenomic imprintingRetinol-Binding Proteins PlasmaHeLa Cells
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Chemoselective Dual Labeling of Native and Recombinant Proteins

2017

The attachment of two different functionalities in a site-selective fashion represents a great challenge in protein chemistry. We report site specific dual functionalizations of peptides and proteins capitalizing on reactivity differences of cysteines in their free (thiol) and protected, oxidized (disulfide) forms. The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups. In order to ensure broader applicability of the functionalization strategy, a novel, short peptide sequence that introduces a disulfide bridge was designed and site-selective dual labeling in the presenc…

0301 basic medicineModels MolecularBiomedical EngineeringPharmaceutical ScienceBioengineering010402 general chemistry01 natural scienceslaw.inventionCell LineMaleimides03 medical and health scienceschemistry.chemical_compoundMiceBacterial ProteinslawAnimalsHumansReactivity (chemistry)CysteineSulfhydryl CompoundsSulfonesMaleimidePeptide sequenceDual labelingPharmacologychemistry.chemical_classificationStaining and LabelingCommunicationOrganic ChemistryDisulfide bondProteinsCombinatorial chemistryRecombinant Proteins0104 chemical sciencesAllyl CompoundsLuminescent Proteins030104 developmental biologychemistryThiolRecombinant DNASurface modificationInterleukin-2PeptidesBiotechnologyBioconjugate Chemistry
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Characterization of sulfhydryl oxidase from Aspergillus tubingensis

2017

Background Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. Results The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initia…

0301 basic medicineentsyymitBOVINE-MILKThioredoxin reductaselcsh:Animal biochemistryBiochemistrySubstrate Specificitychemistry.chemical_compoundNonribosomal peptide synthesisEnzyme Stabilitylcsh:QD415-436DisulfidesDISULFIDE BONDSPeptide Synthaseschemistry.chemical_classificationbiologyGliotoxinChemistrynonribosomal peptide synthesisHydrogen-Ion ConcentrationGlutathioneFAMILYSOXSglutathione oxidationhomesienetAspergillusBiochemistrySENSITIVITYsecreted sulfhydryl oxidaseOxidoreductasesResearch ArticleDithiol oxidaseCofactorlcsh:Biochemistry03 medical and health sciencesNonribosomal peptideNATURAL-PRODUCTSoksidoreduktaasitBIOSYNTHESISlcsh:QP501-801Molecular Biologysecondary metabolismPURIFICATIONIDENTIFICATION030102 biochemistry & molecular biologyCXXC-MOTIFGlutathioneNIGERluonnonaineet030104 developmental biologyEnzymedithiol oxidasebiology.protein1182 Biochemistry cell and molecular biologyAspergillus tubingensisSecreted sulfhydryl oxidaseSecondary metabolismGlutathione oxidationCysteineBMC Biochemistry
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Electrochemical modifications of proteins: disulfide bonds reduction

2002

International audience; Electrochemical reduction of lysozyme disulfide bonds was achieved at pH between 10 and 11.Below pH 10, no disulfide bond cleavage was observed. At pH higher than 12, the cleavage of disulfide bonds is essentially due to hydrolysis. The addition of denaturant considerably enhanced the performance of the electrochemical device.

030303 biophysicsLysozymeElectrochemistryCleavage (embryo)01 natural sciencesAnalytical Chemistry03 medical and health scienceschemistry.chemical_compoundHydrolysisPolymer chemistry[SDV.IDA]Life Sciences [q-bio]/Food engineeringElectrochemistryOrganic chemistryDenaturation (biochemistry)Disulfide bondsComputingMilieux_MISCELLANEOUSReductionchemistry.chemical_classification0303 health sciencesProtein010401 analytical chemistryDisulfide bondGeneral Medicine[SDV.IDA] Life Sciences [q-bio]/Food engineering0104 chemical sciencesEnzymechemistryYield (chemistry)LysozymeFood Science
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Disulfide- and Multisulfide-Containing Metabolites from Marine Organisms

2011

Aquatic OrganismsMolecular StructureBiochemistryChemistryEnvironmental chemistryDisulfide bondAnimalsMarine BiologyDisulfidesGeneral ChemistryMarine Biology (journal)Chemical Reviews
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Synthesis of a New Disulfide Affinity Adsorbent for Purification of Human Uterine Progesterone Receptor

2005

For purification of the human uterine progesterone receptor, an affinity adsorbent was synthesized in which the specific ligand (16 alpha-ethyl-3-oxo-19nor-androst-4-ene 17 beta-carboxylic acid) was bound to derivatized celulose using a disulfide-group-containing spacer. The purified receptor protein, isolated by reductive cleavage of the disulfide bond, bound the synthetic gestagen R5020 with high affinity (Kd 12.2 nmol/l). The affinity gel was highly efficient. A 24000-fold purification of progesterone receptor with a recovery of 40% could be achieved in a single step within 6 h. By means of dodecyl sulphate/polyacrylamide gel electrophoresis two main polypeptides with molecular weights o…

Binding CompetitiveBiochemistryChromatography Affinitychemistry.chemical_compoundCytosolAdsorptionPregnenedionesProgesterone receptorCentrifugation Density GradientHumansCelluloseReceptorPolyacrylamide gel electrophoresisChromatographyProgesterone CongenersMolecular massUterusDisulfide bondLigand (biochemistry)Resins SyntheticchemistryBiochemistryElectrophoresis Polyacrylamide GelFemaleAdsorptionReceptors ProgesteroneEuropean Journal of Biochemistry
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Chemie an starren Grenzflächen, 12. Reduktionsstudien von an Aerosil kovalent Grenzflächen-gebundenen Azo- und Disulfid-Gruppen

1988

Aerosile mit kovalent verknupften, endstandigen Azo- und Disulfid-Gruppen wurden mit dem Ziele hergestellt, Information uber eine Elektronenubergangs-Abstands-Beziehung bei Elektroreduktionen (und bei anderen Reduktionsvorgangen) zu erhalten. Die Grenzflachen-modifizierten Aerosile A–H, J und N wurden hergestellt. Die modifizierten Aerosile A–H und J mit einer ausreichend hohen Belegungsdichte wurden polarographisch untersucht und die erhaltenen Werte mit den Halbstufenpotentialen der homogen gelosten Analogverbindungen verglichen (Tab. 3). Mit einigem Vorbehalt sprechen die Ergebnisse dafur, das Elektronen Abstande von 10–15 A uberwinden konnen. Chemistry on Rigid Interfaces, 12. — Reducti…

ChemistryCovalent bondHomogeneousOrganic ChemistryPolymer chemistryDisulfide bondPhysical and Theoretical ChemistryLiebigs Annalen der Chemie
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Reactions of azoesters and dimethyl acetylenedicarboxylate with 3-methyl-1,2,4-triazole-5-thione

1991

The addition of dimethyl acetylenedicarboxylate to 3-methyl-1,2,4-triazole-5-thione (1), both in alcoholic medium and in inert solvents, has been investigated. When 1 was allowed to react with diethyl azodicarboxylate a disulfide 5 was obtained.

Dimethyl acetylenedicarboxylateDiethyl azodicarboxylatechemistry.chemical_compoundAzo compoundchemistryOrganic ChemistryDisulfide bond124-TriazoleMedicinal chemistryJournal of Heterocyclic Chemistry
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Electrochemical Formation of 3,5-Diimido-1,2-dithiolanes by Dehydrogenative Coupling

2018

A synthetic approach to the cyclic disulfide moiety of 3,5-diimido-1,2-dithiolane derivatives starting with readily available precursors including the electrochemical coupling of dithioanilides is developed. The electrochemical key step provides sustainable synthetic access in high yields, using a very simple electrolysis setup.

Electrolysis010405 organic chemistryChemistryOrganic ChemistryDisulfide bond010402 general chemistryElectrochemistry01 natural sciencesBiochemistryCombinatorial chemistry0104 chemical scienceslaw.inventionCoupling (electronics)lawMoietyPhysical and Theoretical ChemistryOrganic Letters
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Evidence for the attachment of Hsp150/Pir2 to the cell wall of Saccharomyces cerevisiae through disulfide bridges.

2001

Here we present evidence that Hsp150/Pir2, a member of the Pir family of cell wall proteins, can be extracted from the purified cell walls of Saccharomyces cerevisiae by treatment with beta-mercaptoethanol, demonstrating that at least part of this protein is attached to the cell wall through disulfide bridges. We also present evidence that Pir4, another member of this family, is partly secreted to the growth medium. Finally we propose a hypothesis to explain the relationship between the differently localized forms of particular members of the Pir family of cell wall proteins.

Growth mediumSaccharomyces cerevisiae ProteinsbiologySaccharomyces cerevisiaeDisulfide bondGeneral MedicineSaccharomyces cerevisiaebiology.organism_classificationApplied Microbiology and BiotechnologyMicrobiologyCell wallFungal Proteinschemistry.chemical_compoundchemistryBiochemistryCell WallDisulfides2-MercaptoethanolHeat-Shock ProteinsGlycoproteinsMercaptoethanolFEMS yeast research
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