Search results for "Dialysis tubing"

showing 3 items of 3 documents

Disulfide bridge formation between C1q and IgG in vitro.

1990

The globular heads of C1q are known to possess free-SH groups. Here we show that these groups, which are concealed in the native molecule, are exposed by interaction of C1q with dialysis membrane. During iodination, I+ and I2 oxidize these sulfhydryls to produce disulfide-linked C1q aggregates. Approximately 15% of C1q bound to immunoglobulin aggregates is resistant to high conductivity elution and reducing agent is required to release it. These data show that dialysis, adsorption to Ig and iodination of C1q result in structural and functional changes in the molecule, and suggest a mechanism by which these changes occur. Disulfide bridging between C1q and IgG in vitro suggests that this may…

MaleReducing agentImmunologyGuinea Pigschemical and pharmacologic phenomenaBiologyIn Vitro Techniquesurologic and male genital diseasesDialysis tubingfluids and secretionsimmune system diseasesImmunology and AllergyAnimalsSulfhydryl Compoundsskin and connective tissue diseasesComplement C1qComplement ActivationGel electrophoresisComplement C1qIn vitroBiochemistryImmunoglobulin Gbiology.proteinElectrophoresis Polyacrylamide GelFemaleAntibodyDialysis (biochemistry)CysteineEuropean journal of immunology
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Dialysis of flavour compounds: Yields of extraction on model solution

1993

The extraction of 58 flavour compounds by Nafion membrane dialysis was studied using a model solution. Reproducibility and yield of the method were investigated. The coefficient of variation of the extraction yield was less than 15% for 48 of the 58 compounds tested. When the number of carbon atoms increased, the extraction yield fell to zero for compounds with more than ten carbon atoms. Flavour compounds with a cyclic structure showed a better diffusion rate through the membrane than other compounds with the same number of carbon atoms. The extraction yield seems to be correlated mainly to the hydrophobicity of the molecule. The use of the method for quantitative analysis was studied. Ext…

STRUCTURE030309 nutrition & dietetics[SDV]Life Sciences [q-bio]Flavourchemistry.chemical_elementBiochemistryIndustrial and Manufacturing EngineeringDialysis tubing03 medical and health sciences0404 agricultural biotechnologyMoleculeComputingMilieux_MISCELLANEOUS0303 health sciencesChromatographyChemistryExtraction (chemistry)04 agricultural and veterinary sciencesGeneral Chemistry040401 food science[SDV] Life Sciences [q-bio]MembraneYield (chemistry)Condensed Matter::Strongly Correlated ElectronsDialysis (biochemistry)CarbonFood ScienceBiotechnologyZeitschrift f�r Lebensmittel-Untersuchung und -Forschung
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Structure of calcium and zinc pectinate films investigated by FTIR spectroscopy

2010

International audience; Calcium and zinc pectinate gels were prepared using a method which allowed calcium or zinc to diffuse from the cross-linking solution through a dialysis membrane to form a gel with amidated low-methoxyl pectin. The gel thus obtained was then dried, and the film structure was studied using FTIR spectroscopy as a function of the cation content (0%, 5%, 10%, and 15% w/v). Important consideration was given to the three functional groups (amide, carboxyl ester, and carboxylate groups) present in the pectin. When the zinc content was increased, the three wavenumber values corresponding to these three functional groups did not change significantly, while for calcium pectina…

food.ingredientPectinCoordination numberInorganic chemistrychemistry.chemical_elementZincCalciumBiochemistryAnalytical ChemistryDialysis tubingchemistry.chemical_compoundfoodX-Ray DiffractionAmideSpectroscopy Fourier Transform InfraredCarboxylateFourier transform infrared spectroscopyFilmChemistryOrganic ChemistryGeneral MedicinePectin[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsZincFTIR spectroscopyMicroscopy Electron ScanningPectinsCalcium[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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