Search results for " guanidinium chloride"

showing 2 items of 2 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
researchProduct

Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins.

2015

Human Hsp60 chaperonin and its bacterial homolog GroEL, in association with the corresponding co-chaperonins Hsp10 and GroES, constitute important chaperone systems promoting the proper folding of several mitochondrial proteins. Hsp60 is also currently described as a ubiquitous molecule with multiple roles both in health conditions and in several diseases. Naïve Hsp60 bearing the mitochondrial import signal has been recently demonstrated to present different oligomeric organizations with respect to GroEL, suggesting new possible physiological functions. Here we present a combined investigation with circular dichroism and small-angle X-ray scattering of structure, self-organization, and sta…

guanidiniun chloride0301 basic medicineGuanidinium chlorideSmall AngleCircular dichroismBiophysicsmacromolecular substancesBiochemistryGroELChaperoninScatteringMitochondrial Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsX-Ray DiffractionScattering Small AngleHumansGuanidinebiologyProtein StabilityCircular DichroismOrganic ChemistryTemperatureGroESSAXSChaperonin 60Hsp60GroELSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CDcited By 5enzymes and coenzymes (carbohydrates)Denaturation030104 developmental biologychemistryBiochemistryChaperone (protein)biological sciencesbiology.proteinCD; Denaturation; GroEL; Guanidinium chloride; Hsp60; SAXS; Bacterial Proteins; Chaperonin 60; Circular Dichroism; Humans; Mitochondrial Proteins; Protein Stability; Scattering Small Angle; Temperature; X-Ray DiffractionbacteriaHSP60Guanidinium chlorideBiophysical chemistry
researchProduct