Search results for " glycoprotein"

showing 10 items of 430 documents

Review: Applications of HPLC–MS for food analysis

2012

HPLC–MS applications in the agrifood sector are among the fastest developing fields in science and industry. The present tutorial mini-review briefly describes this analytical methodology: HPLC, UHPLC, nano-HPLC on one hand, mass spectrometry (MS) and tandem mass spectrometry (MS/MS) on the other hand. Analytical results are grouped together based on the type of chemicals analyzed (lipids, carbohydrates, glycoproteins, vitamins, flavonoids, mycotoxins, pesticides, allergens and food additives). Results are also shown for various types of food (ham, cheese, milk, cereals, olive oil and wines). Although it is not an exhaustive list, it illustrates the main current directions of applications. …

Mass spectrometry HPLC–MS Food analysis Pesticides Wine Flavonoids Glycoproteins
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A genome-wide association study of marginal zone lymphoma shows association to the HLA region

2015

Marginal zone lymphoma (MZL) is the third most common subtype of B-cell non-Hodgkin lymphoma. Here we perform a two-stage GWAS of 1,281 MZL cases and 7,127 controls of European ancestry and identify two independent loci near BTNL2 (rs9461741, P=3.95 × 10−15) and HLA-B (rs2922994, P=2.43 × 10−9) in the HLA region significantly associated with MZL risk. This is the first evidence that genetic variation in the major histocompatibility complex influences MZL susceptibility.

Medicin och hälsovetenskapLymphomaResearch Support U.S. Gov't P.H.S.Follicular lymphomaGeneral Physics and AstronomyGenome-wide association studyMarginal ZoneP.H.S.Medical and Health SciencesMajor Histocompatibility ComplexPolymorphism (computer science)Non-U.S. Gov'tGENE-EXPRESSIONCELL DEVELOPMENTGeneticsMultidisciplinaryMembrane GlycoproteinsResearch Support Non-U.S. Gov'tSingle NucleotideMarginal zone3. Good healthMultidisciplinary SciencesScience & Technology - Other TopicsNON-HODGKIN-LYMPHOMASUSCEPTIBILITY LOCIGenotypeCèl·lules BEuropean Continental Ancestry GroupEPIDEMIOLOGIC RESEARCHHuman leukocyte antigenBiologyResearch SupportPolymorphism Single NucleotideCLASSIFICATIONGeneral Biochemistry Genetics and Molecular BiologyWhite PeopleArticleN.I.H.Research Support N.I.H. ExtramuralMarginal zone lymphomaMD MultidisciplinaryGenetic variationmedicineJournal ArticleHumansPolymorphismGASTRIC LYMPHOMAIntramuralB cellsScience & TechnologyButyrophilinsGastric lymphomaB-CellExtramuralComputational BiologyGeneral ChemistryLymphoma B-Cell Marginal ZoneResearch Support N.I.H. Intramuralmedicine.diseaseRISK LOCIRHEUMATOID-ARTHRITISLymphomaMalaltia de HodgkinImmunologyU.S. Gov'tHodgkin's diseaseFOLLICULAR LYMPHOMAGenome-Wide Association Study
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Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.

1990

High resolution HPLC techniques such as affinity chromatography (AC), ion exchange chromatography (IEC), and size exclusion chromatography (SEC) were used successfully for separations of hydrophobic plasma membrane glycoproteins. We have tested a lot of commercially available columns for IEC and SEC and performed the purification of the crude plasma membrane extract with the most suitable columns. By using immobilized ligands with different specificities and sequential affinity chromatography, it is possible to obtain a preliminary structural characterization of the interesting carbohydrate residues of membrane glycoproteins.

Membrane GlycoproteinsChromatographyChemistryHealth Toxicology and MutagenesisHydrophilic interaction chromatographyCell MembraneIon chromatographyPublic Health Environmental and Occupational HealthReversed-phase chromatographyChromatography Ion ExchangeHigh-performance liquid chromatographyDisplacement chromatographyChromatography AffinityAffinity chromatographyEvaluation Studies as TopicProtein purificationChromatography GelHumansChromatography columnChromatography High Pressure LiquidResearch ArticleCell Line TransformedEnvironmental Health Perspectives
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Metabolism of Saccharomyces cerevisiae envelope mannoproteins.

1982

By pulse and chase labeling experiments, two independent mannoprotein pools have been found associated with the Saccharomyces cerevisiae envelope. One of them probably corresponds to mannoproteins localized in the periplasmic space. These molecules showed a high turnover rate at 28 degrees C. The second pool is formed by intrinsic wall mannoproteins which are apparently stable for long periods of time, after a small initial turnover. These results suggest that at least part of the mannoproteins initially found in the periplasmic space may move into the wall. The time lag between the addition of the radioactive precursors and their incorporation in the cell envelope (20-30 min for amino acid…

Membrane GlycoproteinsGlucan Endo-13-beta-D-GlucosidaseSaccharomyces cerevisiaeGeneral MedicineMetabolismPeriplasmic spaceSaccharomyces cerevisiaeBiologybiology.organism_classificationBiochemistryMicrobiologyYeastcarbohydrates (lipids)Cell wallFungal ProteinsMannansKineticsBiochemistryCell WallGeneticsBiophysicsMolecular BiologyEnvelope (waves)GlycoproteinsArchives of microbiology
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Research on complement: old issues revisited and a novel sphere of influence

2003

Immunology in recent years has taken a somewhat surprising turn, expressed by a renewed interest in innate immunity. Especially intriguing is the regulatory role exerted by the innate components on the adaptive response, with Toll receptors and complement components being the most investigated. This function has been firmly established for complement protein CR2 (CD21) as part of the BCR co-receptor CD19/CD21/CD81. New findings are now providing a broader picture of complement and its tuning of the immune response; for example, complement proteins have been implicated in the control of T-cell-mediated responses. We will review some of these data here and summarize new discoveries in areas o…

Membrane GlycoproteinsInnate immune systemT-LymphocytesImmunologychemical and pharmacologic phenomenaComplement System ProteinsComplement C1 Inactivator ProteinsBiologyImmunity InnateComplement componentsComplement systemComplement (complexity)Membrane Cofactor ProteinImmune systemAntigens CDComplement Factor HImmunologyAnimalsHumansImmunology and AllergyKidney DiseasesSphere of influenceComplement C1 Inhibitor ProteinSerpinsTrends in Immunology
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Inhibition of the dimorphic transition of Candida albicans by the ornithine decarboxylase inhibitor 1,4-diaminobutanone: alterations in the glycoprot…

1990

Hyphal development in Candida albicans was selectively blocked by the ornithine decarboxylase competitive inhibitor 1,4-diaminobutanone (DAB). Inhibition of hyphal development required DAB during both yeast inoculum growth and subsequent incubation at 37 degrees C to induce mycelial growth. This effect was not due to general growth inhibition since DAB did not inhibit yeast growth, and reduced protein synthesis by 30% at most. Moreover, protein synthesis was unaffected by DAB when cells were pre-grown in drug-containing media. Since DAB inhibited dimorphic transition at 37 degrees C, morphology- and temperature-dependent protein synthesis could be distinguished. DAB stimulated the synthesis…

Membrane GlycoproteinsOrnithine Decarboxylase InhibitorsBiologybiology.organism_classificationMicrobiologyMolecular biologyYeastOrnithine decarboxylaseFungal Proteinschemistry.chemical_compoundchemistryBiochemistryOrnithine Decarboxylase InhibitorCell WallEnzyme inhibitorCandida albicansPutrescinebiology.proteinProtein biosynthesisGrowth inhibitionCandida albicansPolyamineJournal of General Microbiology
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CD28, a marker associated with tumoral expansion in multiple myeloma

1998

International audience; CD28 expression was thoroughly investigated on plasma cells of monoclonal gammopathy of undetermined significance, multiple myeloma (MM), and human myeloma cell lines. CD28+ plasma cells were detected in 19% of 31 monoclonal gammopathy of undetermined significance, 41% of 116 MM, and 100% of 13 human myeloma cell lines. CD28+ myeloma cells were detected in 21 of 79 (26%) MM cases at diagnosis, 13 of 22 (59%) at medullary relapse (P < 0.009), and 14 of 15 (93%) at extramedullary relapse (P = 0.05), including 10 of 10 (100%) secondary plasma cell leukemias (P = 0.05). Serial studies in individual patients confirmed the emergence of CD28+ myeloma cells with tumoral expa…

Membrane GlycoproteinsParaproteinemiasNeoplasms Second Primarychemical and pharmacologic phenomenahemic and immune systemsCD56 AntigenCell LineLeukemia Plasma CellCD28 AntigensAntigens CDBone MarrowPredictive Value of TestsRecurrence[ INFO.INFO-BI ] Computer Science [cs]/Bioinformatics [q-bio.QM]hemic and lymphatic diseasesB7-1 AntigenBiomarkers TumorDisease ProgressionTumor Cells CulturedHumansB7-2 AntigenTreatment Failure[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Multiple Myeloma[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]
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Identification of a 49-kDa hydrophobic cell wall mannoprotein present in velum yeast which may be implicated in velum formation

2000

Analysis of velum-forming yeast cell wall components released by beta-1,3-glucanase treatment were compared with those of a non velum-forming yeast. SDS-PAGE electrophoresis and Western blotting with ConA-peroxidase staining of mannoproteins allowed us to identify a 49-kDa mannoprotein present in the cell wall of the velum-forming yeast and hardly visible in the control. The cell wall nature of this protein was confirmed by labelling with the non-permeable sulfosuccinimydiyl-6-(biotinamido)hexanoate reagent. A partial purification of this mannoprotein by anion exchange HPLC followed by surface hydrophobicity determination revealed that the fraction containing the 49-kDa mannoprotein was the…

Membrane GlycoproteinsSurface PropertiesBlotting WesternCellWineSaccharomyces cerevisiaeBiologyMicrobiologyYeastStainingFungal Proteinscarbohydrates (lipids)BlotCell wallElectrophoresismedicine.anatomical_structureBiochemistryCell WallBiotinylationGeneticsmedicineBiotinylationElectrophoresis Polyacrylamide GelMolecular BiologyPolyacrylamide gel electrophoresisFEMS Microbiology Letters
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Serologic Response to Cell Wall Mannoproteins and Proteins of Candida albicans

1998

SUMMARY The cell wall of Candida albicans not only is the structure in which many biological functions essential for the fungal cells reside but also is a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both the carbohydrate and protein moieties are able to trigger immune responses. Although cell-mediated immunity is often considered to be the most important line of defense against candidiasis, cell wall protein and glycoprotein components also elicit a potent humoral response from the host that may include some protective antibodies. Prot…

Microbiology (medical)Antigens FungalEpidemiologyBiologyArticleMicrobiologyFungal ProteinsImmune systemAntigenCell WallCandida albicansAnimalsHumansCandida albicanschemistry.chemical_classificationFungal proteinMembrane GlycoproteinsGeneral Immunology and MicrobiologyPublic Health Environmental and Occupational Healthbiology.organism_classificationBacterial adhesinInfectious DiseaseschemistryHumoral immunityImmunologybiology.proteinAntibodyGlycoproteinClinical Microbiology Reviews
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Diagnosis of systemic candidiasis by enzyme immunoassay detection of specific antibodies to mycelial phase cell wall and cytoplasmic candidal antigens

1993

Diagnosis of systemic Candida infections was attempted by the use of an enzyme-linked immunosorbent assay (EIA) to detect IgG antibodies towards cell wall-bound and cytoplasmic candidal antigens. Cell wall antigens were sequentially solubilized by treatment of germinated blastoconidia of Candida albicans (ATCC 26555 strain) with beta-mercaptoethanol (beta ME extract) and digestion with Zymolyase 20T, a beta-glucanase preparation (Zymolyase extract). Protoplasts obtained after treatment with Zymolyase were osmotically lysed (cytoplasmic antigens). Sera were obtained from patients with systemic (n = 28) and superficial (n = 46) candidiasis. Control sera were obtained from normal healthy indiv…

Microbiology (medical)CytoplasmAntigens FungalBlotting WesternEnzyme-Linked Immunosorbent AssaySensitivity and SpecificityBlastoconidiumMicrobiologyFungal ProteinsMannansAntigenCell WallCandida albicansmedicineHumansCandida albicansAntibodies FungalMannanMembrane Glycoproteinsbiologymedicine.diagnostic_testCandidiasisGeneral Medicinebiology.organism_classificationmedicine.diseaseCorpus albicansInfectious DiseasesImmunoglobulin GImmunoassaybiology.proteinSystemic candidiasisAntibodyLatex Fixation TestsEuropean Journal of Clinical Microbiology &amp; Infectious Diseases
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