Search results for "Endoglycosidase H"

showing 4 items of 4 documents

The IgGFc-binding protein FCGBP is secreted with all GDPH sequences cleaved but maintained by interfragment disulfide bonds

2021

Mucus forms an important protective barrier that minimizes bacterial contact with the colonic epithelium. Intestinal mucus is organized in a complex network with several specific proteins, including the mucin-2 (MUC2) and the abundant IgGFc-binding protein, FCGBP. FCGBP is expressed in all intestinal goblet cells and is secreted into the mucus. It is comprised of repeated von Willebrand D (vWD) domain assemblies, most of which have a GDPH amino acid sequence that can be autocatalytically cleaved, as previously observed in the mucins MUC2 and mucin-5AC. However, the functions of FCGBP in the mucus are not understood. We show that all vWD domains of FCGBP with a GDPH sequence are cleaved and …

0301 basic medicineMUC5AC mucin-5ACMUC2 mucin-2 (Muc2 mouse)vWF von Willebrand factorBiochemistryvon Willebrand domainchemistry.chemical_compoundPVDF polyvinylidene difluorideMiceCricetinaeDisulfidesIntestinal MucosaPeptide sequenceEndoH endoglycosidase HbiologyChemistryrespiratory systemGDPH Gly-Asp-Pro-HisChaotropic agentBiochemistryWB Western blotIodoacetamideGuHCl guanidinium chlorideResearch ArticleIgG immunoglobulin GvWD von Willebrand D domainCHO CellsCHO Chinese hamster ovary03 medical and health sciencesEndoglycosidase HCricetulusProtein Domainsmucusvon Willebrand FactorAnimalsHumansintestinal epitheliumMolecular BiologyintestineFCGBP IgGFc-binding protein (Fcgbp mouse)GAPH Gly-Ala-Pro-HisMucin-2030102 biochemistry & molecular biologycolonBinding proteinEndoplasmic reticulumMucinITH3 inter-alpha-trypsin inhibitor heavy chain 3Cell BiologyMucusMice Inbred C57BL030104 developmental biologyMUC2Proteolysisbiology.proteinImmunoglobulin G (IgG)IAA iodoacetamideCell Adhesion MoleculesdisulfideThe Journal of Biological Chemistry
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Secretion, interaction and assembly of two O-glycosylated cell wall antigens from Candida albicans.

2001

The mechanisms of incorporation of two antigens have been determined using a monoclonal antibody (3A10) raised against the material released from the mycelial cell wall by zymolyase digestion and retained on a concanavalin A column. One of the hybridomas secreted an IgG that reacted with two bands in Western blots. Indirect immunofluorescence showed that the antigens were located on the surfaces of mycelial cells, but within the cell walls of yeasts. These antigens were detected in a membrane preparation, in the SDS-soluble material and in the material released by a 1,3-beta-glucanase and chitinase from the cell walls of yeast and mycelial cells. In the latter three samples, an additional h…

Antigens FungalGlycosylationbeta-GlucansMicrobiologyCell wallEndoglycosidase Hchemistry.chemical_compoundMiceAntigenChitinCell WallCandida albicansAnimalsSecretionFluorescent Antibody Technique IndirectGlucansAntibodies FungalMice Inbred BALB CMembrane GlycoproteinsbiologyAntibodies MonoclonalMolecular biologyBiochemistrychemistryConcanavalin AChitinasebiology.proteinFemaleAntibodyMicrobiology (Reading, England)
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Effect of α-factor on individual wall mannoproteins fromSaccharomyces cerevisiae acells

1985

Treatment of Saccharomyces cerevisiae a cells with α-factor partially inhibits mannosylation of the high Mr mannoproteins, although there is an increase in the total amount of these molecules present in the wall. They show a similar mobility in SDS-acrylamide gels to those from untreated mnn2 cells. No other significant effects on wall mannoproteins have been observed, except a decrease in the amount of the 29 kDa species.

Gel electrophoresisbiologySaccharomyces cerevisiaebiology.organism_classificationMicrobiologyYeastcarbohydrates (lipids)Cell wallAgglutination (biology)Endoglycosidase Hchemistry.chemical_compoundBiochemistrychemistryMannosylationAcrylamideGeneticsbiology.proteinMolecular BiologyFEMS Microbiology Letters
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The catalytic activity of the endoplasmic reticulum-resident protein microsomal epoxide hydrolase towards carcinogens is retained on inversion of its…

1996

Diol epoxides formed by the sequential action of cytochrome P-450 and the microsomal epoxide hydrolase (mEH) in the endoplasmic reticulum (ER) represent an important class of ultimate carcinogenic metabolites of polycyclic aromatic hydrocarbons. The role of the membrane orientation of cytochrome P-450 and mEH relative to each other in this catalytic cascade is not known. Cytochrome P-450 is known to have a type I topology. According to the algorithm of Hartman, Rapoport and Lodish [(1989) Proc. Natl. Acad. Sci. U.S.A. 86, 5786–5790], which allows the prediction of the membrane topology of proteins, mEH should adopt a type II membrane topology. Experimentally, mEH membrane topology has been …

GlycosylationGlycosylation1303 BiochemistryCytochromeStereochemistryMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthEndoplasmic ReticulumBiochemistryCatalysis1307 Cell Biologychemistry.chemical_compoundEndoglycosidase H1312 Molecular BiologyAnimalsAmino Acid SequenceBenzopyrenesMolecular BiologyEpoxide HydrolasesbiologyEndoplasmic reticulumCell BiologyIntracellular MembranesRecombinant ProteinsRatsCytosolMembranechemistryMicrosomal epoxide hydrolaseMembrane topologyCOS Cellsbiology.proteinCarcinogensMutagenesis Site-Directed570 Life sciences; biologyResearch Article
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