Search results for "Acetylglucosaminidase"

showing 10 items of 14 documents

The extracellular wall-bound β-N-acetylglucosaminidase from Lactobacillus casei is involved in the metabolism of the human milk oligosaccharide lacto…

2015

Human milk oligosaccharides (HMOs) are considered to play a key role in establishing and maintaining the infant gut microbiota. Lacto-N-triose forms part of both type 1 and type 2 HMOs and also of the glycan moieties of glycoproteins. Upstream of the previously characterized gene cluster involved in lacto-N-biose and galacto-N-biose metabolism from Lactobacillus casei BL23, there are two genes, bnaG and manA, encoding a β-N-acetylglucosaminidase precursor and a mannose-6-phosphate isomerase, respectively. In this work, we show that L. casei is able to grow in the presence of lacto-N-triose as a carbon source. Inactivation of bnaG abolished the growth of L. casei on this oligosaccharide, dem…

0301 basic medicineLactobacillus caseiGlycan030106 microbiologyMutantMannoseOligosaccharidesGenetics and Molecular BiologyApplied Microbiology and BiotechnologyMicrobiology03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsCell WallAcetylglucosaminidaseHumanschemistry.chemical_classificationEcologybiologyMilk Humanfood and beveragesOligosaccharidebiology.organism_classificationEnzyme assayLacticaseibacillus caseiEnzymechemistryBiochemistrybiology.proteinGlycoproteinTrisaccharidesFood ScienceBiotechnology
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Activities of some antioxidative and hexose monophosphate shunt enzymes of skeletal muscle in neuromuscular diseases.

1986

The activities of some antioxidative and hexose monophosphate shunt enzymes, as well as of 2 hydrolases were studied in skeletal muscle biopsy specimens taken from 39 patients with neuromuscular diseases and from 15 controls. The activity of Se-dependent glutathione peroxidase was higher in patients with congenital myotonia, whereas in the other diagnostic groups this enzyme activity was the same as in the controls. The Se-independent and total glutathione peroxidase activity of patients in the various diagnostic groups did not differ from the controls. Moreover, no difference were observed in catalase activity between the patient groups and the controls. The activities of the rate limiting…

Adultmedicine.medical_specialtyAdolescentDehydrogenasePentose phosphate pathwayGlucosephosphate DehydrogenaseInternal medicineAcetylglucosaminidasemedicineHumansAgedchemistry.chemical_classificationGlutathione PeroxidaseMuscle biopsybiologymedicine.diagnostic_testGlutathione peroxidaseMusclesPhosphogluconate DehydrogenaseSkeletal muscleGeneral MedicineNeuromuscular DiseasesSyndromeMiddle AgedCatalaseEnzyme assayMuscle atrophymedicine.anatomical_structureEndocrinologyNeurologychemistrybiology.proteinNeurology (clinical)medicine.symptomPeroxidasePeptide HydrolasesActa neurologica Scandinavica
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Glycoprotein molecules in the walls of Schizosaccharomyces pombe wild-type cells and a morphologically altered mutant resistant to papulacandin B

1990

SUMMARY: Schizosaccharomyces pombe cell walls contain two major glycoprotein species, I and II, with molecular masses of 2 x 106 and 5 x 105 Da respectively, as determined by gel filtration chromatography and PAGE. The ratio of sugar to protein is higher in species I than in species II. Much of the sugar in both glycoproteins (about 85% in wild-type cells) is O-linked to the peptide moiety. The morphological sph1 mutant is resistant to papulacandin B, and its cell wall contains less glycoprotein II (but not less glycoprotein I) than the parental wild-type strain, although glycoprotein II is still synthesized and released into the growth medium. Papulacandin B largely reverses the morphologi…

Antifungal AgentsHydrolasesMutantCarbohydratesDrug ResistancePapulacandin BBiologyCell morphologyMicrobiologyCell wallchemistry.chemical_compoundCell WallAcetylglucosaminidaseSchizosaccharomycesGlycoproteinsGel electrophoresischemistry.chemical_classificationWild typebiology.organism_classificationAnti-Bacterial AgentsCulture MediaMolecular WeightAminoglycosidesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseSolubilityBiochemistrychemistryMutationSchizosaccharomyces pombeChromatography GelGlycoproteinJournal of General Microbiology
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Effect of freezing/thawing process in different sizes of blue fish in the Mediterranean through lysosomal enzymatic tests

2014

The assessment of freshness of different sizes of blue fish (Engraulis encrasicolus 12 cm, Sardina pilchardus 15 cm, Trachurus trachurus 40 cm, Scomber japonicus colias 60 cm) was carried out using non-conventional enzymatic methods. The activities of the three lysosomal enzymes (α-glucosidase (AG), β-galactosidase (B-GAL) and β-N-acetylglucosamidase (B-NA)) in extracts of blue fish muscle were measured over a period of 21 days of storage. A significant increase (p < 0.05) of AG activity was observed in all species, with a large increase seen after only one day of storage. B-NA activity increased slightly in sardines, horse mackerels and chub mackerel during frozen/thawed storage. Finally, …

Food HandlingFood storageBlue fishAnalytical ChemistryColiasEngraulisCommercial fraudChub mackerelAcetylglucosaminidaseFreezingBLUE FISH; ENZYMES; SHELF LIFEAnimalsFood scienceTrachurus trachurusβ-Galactosidase (B-GAL)ScomberbiologyMediterranean RegionMusclesFishesHorsealpha-GlucosidasesGeneral MedicineSettore AGR/15 - Scienze E Tecnologie Alimentariα-Glucosidase (AG)beta-Galactosidasebiology.organism_classificationHorse mackerelFisheryβ-N-acetylglucosamidase (B-NA)Food StorageSeafoodSHELF LIFEFreeze/thawingLysosomesENZYMESFood Science
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The second component of human complement: Use of glycosidases and glucosylation to distinguish the two forms

1988

Abstract The two forms of human plasma C2 that were described in the preceding report (1) were investigated for their functional and biochemical differences. Incubation with the neuraminidase (NAN'dase) of Clostridium perfringens at 37°C resulted in a four- to fivefold increase in the hemolytic activity of both forms. The increase in activity was different than the increase caused by treatment with iodine. The mechanism of increased activity of NAN'dase-treated C2 was the generation of increased molecules of activated C3 (C3b), resulting in more molecules of C5 binding to (C4b, 2a, 3b)n. Removal of N-acetyl-neuraminate from C2 did not alter its binding to a cationic exchanger. Nonenzymatic …

GlycosylationGlycoside HydrolasesbiologyChemistryImmunologyCationic polymerizationNeuraminidaseHematologyComplement C2Clostridium perfringensFree aminomedicine.disease_causeIn vitroKineticsBiochemistryHuman plasmaN acetylglucosaminidasebiology.proteinmedicineHumansImmunology and AllergyIncubationNeuraminidaseIodineImmunobiology
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Candida albicans mycelial wall structure: supramolecular complexes released by zymolyase, chitinase and beta-mercaptoethanol.

1991

Different techniques released from the wall of Candida albicans mycelial cells high molecular weight mannoprotein materials with different levels of complexity. SDS solubilized among others one protein of 180 kDa which reacted with a monoclonal antibody (MAb) specific of a O-glycosylated protein secreted by regenerating mycelial protoplasts [Elorza et al. (1989) Biochem Biophys Res Commun 162:1118-1125]. Zymolyase, chitinase and beta-mercaptoethanol, released different types of high molecular highly polydisperse mannoprotein materials (greater than 180 kDa) that also reacted with the same MAb. These materials had N-glycosidically linked sugar chains, in addition to the O-glycosidically bond…

HydrolasesBlotting WesternMannoseGerm tubeChitinBiologyBiochemistryMicrobiologyCell wallchemistry.chemical_compoundChitinCell WallCandida albicansGeneticsSodium dodecyl sulfateCandida albicansMolecular BiologyPolyacrylamide gel electrophoresisMembrane GlycoproteinsHydrolysisChitinasesSodium Dodecyl SulfateGeneral Medicinebiology.organism_classificationcarbohydrates (lipids)Microscopy ElectronHexosaminidasesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidasechemistryBiochemistrySolubilityChitinasebiology.proteinChromatography GelElectrophoresis Polyacrylamide GelArchives of microbiology
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Quantitative studies of the secretion of complement component C3 by resident, elicited and activated macrophages. Comparison with C2, C4 and lysosoma…

1982

To quantitate the secretion of complement component C3 by guinea pig peritoneal macrophages an enzyme-linked immunosorbent assay was developed. C3 secretion was studied in resident, elicited and activated macrophages and compared with release of hemolytically active C2 and C4, as well as the lysosomal enzyme β-D-2-acetamido-2-deoxyglucosidase. Resident macrophages secreted about 6 ng C3/106 cells/h into culture supernatants over a period of 12 h. Corynebacterium parvum-activated cells were found to secrete 3 times that amount at nearly constant rates. There was a stepwise increase in secretion of functional C2 and C4 when comparing resident, elicited and activated macrophages; secretion was…

ImmunologyEnzyme releaseGuinea PigsCorynebacteriumEnzyme-Linked Immunosorbent AssayHemolysisGuinea pigAcetylglucosaminidaseImmunology and AllergyAnimalsHumansSecretionPropionibacterium acnesSerum Albuminchemistry.chemical_classificationbiologyMacrophagesComplement C4Complement C3Complement C2Macrophage Activationbiology.organism_classificationMolecular biologyKineticsEnzymechemistryCell culture supernatantLysosomesEuropean journal of immunology
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Exhaustive physical exercise and acid hydrolase activity in mouse skeletal muscle

1978

Adult, untrained NMRI mice were exhausted on a motor-driven treadmill by an intermittent-type running programme. Serial cryostate sections for the staining of NADH-tetrazolium reductase, beta-glucuronidase, beta-N-acetylglucosaminidase, and beta-glycerophosphatase activities and for making hematoxylin-eosin staining were cut from m. quadriceps femoris 1, 2, 3, 5, 7, and 15 days after physical exhaustion. A strong increase in the activities of beta-glucuronidase and beta-N-acetylglucosaminidase was observed 7 days after exhaustion and the activity changes, which were similar for the both glycosidases, were more prominent in the highly oxidative red compared to less oxidative white fibres. Ac…

Malemedicine.medical_specialtyHistologyHydrolasesPhysical ExertionConnective tissuePhysical exerciseBiologyMiceMuscular DiseasesInternal medicineAcetylglucosaminidasemedicineAnimalsMyocyteMolecular BiologyGlucuronidaseHistocytochemistryMusclesNADPH DehydrogenaseSkeletal muscleExtremitiesCell BiologyGeneral MedicinePhosphoric Monoester HydrolasesStainingMedical Laboratory TechnologyEndocrinologymedicine.anatomical_structureBiochemistryGlycerophosphatesbiology.proteinAnatomyGeneral Agricultural and Biological SciencesMyofibrilHomeostasisAcid hydrolaseHistochemistry
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Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities

1978

The activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different tran…

Malemedicine.medical_specialtyPhysiologyAcid PhosphataseCathepsin DCitrate (si)-SynthaseMalate dehydrogenaseElectron Transport Complex IVMicechemistry.chemical_compoundRibonucleasesMalate DehydrogenaseEndurance trainingLactate dehydrogenaseInternal medicineAcetylglucosaminidasemedicineAnimalsCitrate synthaseCytochrome c oxidaseArylsulfatasesGlucuronidaseDeoxyribonucleasesPhysical Education and TrainingL-Lactate DehydrogenasebiologyHistocytochemistryMusclesAcid phosphataseSkeletal muscleCathepsinsEndocrinologymedicine.anatomical_structurechemistryBiochemistrybiology.proteinEnergy MetabolismLysosomesActa Physiologica Scandinavica
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?-Glucuronidase activity in trained red and white skeletal muscle of mice

1978

We studied the effects of prolonged running exercise (5 days a week, 1.5 h per day at a speed of 17.6 m/min) on the activity of some acid hydrolases (beta-glucuronidase, beta-N-acetylglucosaminidase, acid phosphatase and cathepsin D) and three enzymes of energy metabolism (cytochrome c oxidase, lactate dehydrogenase and creatine kinase) in the distal and in the proximal, the predominantly white and red parts, respectively, of the vastus lateralis-muscle from mice. The acid hydrolase activity levels were 1.24--1.69 higher in untrained red muscle compared to untrained white muscle. The light training applied increased the activity of beta-glucuronidase in both red and white muscle. No other s…

Malemedicine.medical_specialtyPhysiologyAcid PhosphataseCathepsin DElectron Transport Complex IVMicechemistry.chemical_compoundPhysical Conditioning AnimalPhysiology (medical)Internal medicineLactate dehydrogenaseAcetylglucosaminidasemedicineAnimalsCytochrome c oxidaseOrthopedics and Sports MedicineCreatine KinaseGlucuronidasechemistry.chemical_classificationL-Lactate DehydrogenasebiologyMusclesPublic Health Environmental and Occupational HealthAcid phosphataseSkeletal muscleGeneral MedicineCathepsinsEnzymeEndocrinologymedicine.anatomical_structurechemistrybiology.proteinCreatine kinaseAcid hydrolaseEuropean Journal of Applied Physiology and Occupational Physiology
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