Search results for "Acetylglucosaminidase"

showing 4 items of 14 documents

Acid hydrolase activity in red and white skeletal muscle of mice during a two-week period following exhausting exercise

1978

The activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, p-nitrophenylphosphatase, and malate dehydrogenase together with protein content were assayed from representative mixed (m. rectus femoris), predominantly red (proximal heads of m. vastus lateralis, m.v. medius and m. v. intermedius), and predominantly white (distal head of m. vastus lateralis) muscle homogenates of mice during a two-week period following one single exposure to exhausting intermittent running on a treadmill. The activities of cathepsin D and beta-glycerophosphatase were assayed from mixed muscle only. In all three muscle types, particularly in red muscle, the activities of beta…

Malemedicine.medical_specialtyTime FactorsHydrolasesPhysiologyAcid PhosphatasePhysical ExertionClinical BiochemistryPhosphataseCathepsin DBiologyMalate dehydrogenaseMiceRibonucleasesMalate DehydrogenasePhysiology (medical)Internal medicineAcetylglucosaminidasemedicineAnimalsTreadmillReceptorArylsulfatasesGlucuronidase4-NitrophenylphosphataseMusclesSkeletal musclebiology.organism_classificationCathepsinsMediusEndocrinologymedicine.anatomical_structurebiology.proteinAcid hydrolasePfl�gers Archiv European Journal of Physiology
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O-glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclero…

2005

Mammalian neurofilaments (NFs) are modified by post-translational modifications that are thought to regulate NF assembly and organization. Whereas phosphorylation has been intensely studied, the role of another common modification, the attachment of O-linked N-acetylglucosamine (GlcNAc) to individual serine and threonine residues, is hardly understood. We generated a novel monoclonal antibody that specifically recognizes an O-glycosylated epitope in the tail domain of NF-M and allows determination of the glycosylation state at this residue. The antibody displays strong species preference for human NF-M, shows some reactivity with rat but not with mouse or bovine NF-M. By immunohistochemistr…

NeurofilamentGlycosylationGlycosylationMolecular Sequence DataHyperphosphorylationBiologyMitogen-activated protein kinase kinaseBiochemistryAnimals Genetically Modifiedchemistry.chemical_compoundEpitopesMiceWestern blotNeurofilament ProteinsCell Line TumorAcetylglucosaminidasemedicineAnimalsHumansAmino Acid SequenceProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase KinasesNeuronsmedicine.diagnostic_testKinaseAmyotrophic Lateral SclerosisAntibodies MonoclonalCell BiologyAxonsCell biologyProtein Structure TertiaryRatsDisease Models AnimalchemistryBiochemistrySpinal CordNIH 3T3 CellsPhosphorylationCattleThe Journal of biological chemistry
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Missense mutations of dual oxidase 2 (DUOX2) implicated in congenital hypothyroidism have impaired trafficking in cells reconstituted with DUOX2 matu…

2007

Abstract Dual oxidase 2 (DUOX2), a reduced NAD phosphate:O2 oxidoreductase flavoprotein, is a component of the thyrocyte H2O2 generator required for hormone synthesis at the apical plasma membrane. We recently identified a specific DUOX2 maturation factor (DUOXA2) that is necessary and sufficient for expression of functional DUOX2 in mammalian cell lines. We have now used a DUOXA2 reconstituted system to provide the first characterization of natural DUOX2 missense variants (Q36H, R376W, D506N) at the molecular level, analyzing their impact on H2O2 generation, trafficking, stability, folding, and DUOXA2 interaction. The Q36H and R376W mutations completely prevent routing of DUOX2 to the cell…

Protein FoldingMutantMutation MissenseBiologyEndoplasmic ReticulumCell membranesymbols.namesakeEndocrinologyMutant proteinPolysaccharidesCalnexinmedicineCongenital HypothyroidismAnimalsHumansMolecular BiologyCells CulturedFlavoproteinsOxidative foldingEndoplasmic reticulumCell MembraneMembrane ProteinsNADPH OxidasesDual oxidase 2General MedicineHydrogen PeroxideGolgi apparatusDual OxidasesRatsProtein Transportmedicine.anatomical_structureMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseBiochemistrysymbolsOxidation-ReductionMolecular endocrinology (Baltimore, Md.)
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Activity of acid hydrolases in skeletal muscle of untrained, trained and detrained mice of different ages.

1978

The activities of p-nitrophenylphosphatase, beta-glucuronidase and beta-N-acetylglucosaminidase from crude skeletal muscle homogenates of 4 and 7 months old mice were assayed after short-term intensive and long-term moderate training and after terminated training. In the older untrained mice the activity of the hydrolases was higher than in the younger mice. The level increased with training and this increase was far more pronounced in the older animals. Cessation of training for 7 and 21 days decreased this activity in the older animals but it was again increased 42 days later and close to the level observed in the trained mice. In young mice 3 days' terminated training increased the activ…

medicine.medical_specialty4-NitrophenylphosphatasePhysiologyCatabolismMuscleseducationPhysical ExertionAge FactorsSkeletal musclePhysiologyMetabolismBiologyPhosphoric Monoester HydrolasesMicemedicine.anatomical_structureHexosaminidasesAcetylglucosaminidasePhysical therapymedicineAnimalsGlucuronidaseActa physiologica Scandinavica
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