Search results for "Teas"

showing 10 items of 619 documents

Laundry detergent compatibility of the alkaline protease from Bacillus cereus.

2004

The endogenous protease activity in various commercially available laundry detergents of international companies was studied. The maximum protease activity was found at 50 degrees C in pH range 10.5-11.0 in all the tested laundry detergents. The endogenous protease activity in the tested detergents retained up to 70% on incubation at 40 degrees C for 1 h, whereas less than 30% activity was only found on incubation at 50 degrees C for 1 h. The alkaline protease from an alkalophilic strain of Bacillus cereus was studied for its compatibility in commercial detergents. The cell free fermented broth from shake flask culture of the organism showed maximum activity at pH 10.5 and 50 degrees C. The…

ProteasesProteasebiologyLaundrymedicine.medical_treatmentDetergentsSerine EndopeptidasesBacillus cereusTemperatureAlkaliesHydrogen-Ion Concentrationbiology.organism_classificationMicrobiologyCereusBiochemistryBacillus cereusmedicineFermentationFood scienceIncubationLaundry detergentMicrobiological research
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Antiproliferative Properties of a Few Auranofin-Related Gold(I) and Silver(I) Complexes in Leukemia Cells and their Interferences with the Ubiquitin …

2020

A group of triethylphosphine gold(I) and silver(I) complexes, structurally related to auranofin, were prepared and investigated as potential anticancer drug candidates. The antiproliferative properties of these metal compounds were assessed against two leukemia cell lines, i.e., CCRF-CEM and its multidrug-resistant counterpart, CEM/ADR5000. Interestingly, potent cytotoxic effects were disclosed for both series of compounds against leukemia cells, with IC50 values generally falling in the low-micromolar range, the gold derivatives being on the whole more effective than the silver analogues. Some initial structure-function relationships were drawn. Subsequently, the ability of the study compo…

ProteasesProteasome Endopeptidase ComplexAuranofinSilverleukemia cellsPharmaceutical Sciencemetal complexesantiproliferative propertiesArticleAnalytical ChemistryMetallcsh:QD241-44103 medical and health sciencesInhibitory Concentration 500302 clinical medicineGold Compoundslcsh:Organic chemistryCell Line TumorDrug DiscoverymedicineCytotoxic T cellHumansPhysical and Theoretical Chemistry030304 developmental biologyCell Proliferationproteasome inhibition0303 health sciencesLeukemiaChemistryUbiquitinOrganic Chemistryauranofinmedicine.diseaseauranofin metal complexes proteasome inhibition leukemia cells antiproliferative propertiesDrug Resistance MultipleLeukemiaProteasomeBiochemistryChemistry (miscellaneous)Drug Resistance Neoplasm030220 oncology & carcinogenesisvisual_artvisual_art.visual_art_mediumauranofin;metal complexes; proteasome inhibition; leukemia cells; antiproliferative propertiesMolecular MedicineGoldSelectivitymedicine.drugMolecules
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The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional diffe…

2006

The procollagen C-proteinase (PCP) is a zinc peptidase of the astacin family and the metzincin superfamily. The enzyme removes the C-terminal propeptides of fibrillar procollagens and activates other matrix proteins. Besides its catalytic protease domain, the procollagen C-proteinase contains several C-terminal CUB modules (named after complement factors C1r and C1s, the sea urchin UEGF protein, and BMP-1) and EGF-like domains. The two major splice forms of the C-proteinase differ in their overall domain composition. The longer variant, termed mammalian tolloid (mTld, i.e., PCP-2), has the protease- CUB1-CUB2-EGF1-CUB3-EGF2-CUB4-CUB5 composition, whereas the shorter form termed bone morphog…

ProteasesProtein FoldingTolloid-Like Metalloproteinasesmedicine.medical_treatmentRNA SplicingBiologyAntiparallel (biochemistry)BiochemistryBone morphogenetic protein 1law.inventionBone Morphogenetic Protein 1lawmedicineAnimalsProtein precursorDNA PrimersProteaseBase SequenceCircular DichroismMetalloendopeptidasesSurface Plasmon ResonanceRecombinant ProteinsProcollagen peptidaseSpectrometry FluorescenceBiochemistryBone Morphogenetic ProteinsRecombinant DNAMetalloproteasesElectrophoresis Polyacrylamide GelAstacinProcollagenBiochemistry
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Investigation of the steps involved in the difference of susceptibility of Ephestia kuehniella and Spodoptera littoralis to the Bacillus thuringiensi…

2011

BUPM95 is a Bacillus thuringiensis subsp. kurstaki strain producing the Vip3Aa16 toxin with an interesting insecticidal activity against the Lepidopteran larvae Ephestia kuehniella. Study of different steps in the mode of action of this Vegetative Insecticidal Protein on the Mediterranean flour moth (E. kuehniella) was carried out in the aim to investigate the origin of the higher susceptibility of this insect to Vip3Aa16 toxin compared to that of the Egyptian cotton leaf worm Spodoptera littoralis. Using E. kuehniella gut juice, protoxin proteolysis generated a major band corresponding to the active toxin and another band of about 22kDa, whereas the activation of Vip3Aa16 by S. littoralis …

ProteasesProteolysismedia_common.quotation_subjectBacillus thuringiensisDrug ResistanceActivationBacillusInsectMothsSpodopteraBiologymedicine.disease_causeMicrobiologyBacterial ProteinsVip3Aa16Bacillus thuringiensismedicineAnimalsPest Control BiologicalSpodoptera littoralisEcology Evolution Behavior and SystematicsEphestia kuehniellamedia_commonmedicine.diagnostic_testToxinfungiSpodoptera littoralisbiology.organism_classificationMediterranean flour mothLarvaBacillusthuringiensisMidgut putative receptorJournal of Invertebrate Pathology
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Detection of proteolytic (C 3-cleaving) activity on mouse mastocytoma (P815) cells and other mouse cell lines by formation of cell contact with C 3-c…

1979

Mouse mastocytoma cells (P 815) formed rosettes with normal mouse spleen lymphocytes which had been coated with uncleaved human C 3; this interaction was clearly dependent on the amount of C 3. Lymphocytes treated with C 3 b or buffer alone were ineffective. Formation of cell contact could be inhibited by the presence of protease inhibitors such as diisopropyl fluorophosphate, phenyl methyl sulfonyl fluoride and tosyllysyl chloromethyl ketone. Seve n out of 13 different cell lines behaved like P 815 cells. The results strongly suggested that a proteolytic activity on mouse tumor cells led to a cooperation with uncleaved C 3 on a carrier cell to connect these two cells. We interpreted these …

ProteasesRosette FormationImmunologyCellMast-Cell SarcomaCell CountBiologyCleavage (embryo)Cell LineCell membraneMicemedicineAnimalsImmunology and AllergyProtease InhibitorsLymphocytesCell MembraneMastocytomaComplement C3medicine.diseaseMolecular biologymedicine.anatomical_structureCell cultureMast cell sarcomaDiisopropyl fluorophosphateSpleenmedicine.drugEuropean Journal of Immunology
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Development of rhodesain inhibitors with a 3-bromoisoxazoline warhead

2013

Novel rhodesain inhibitors were obtained by combining an enantiomerically pure 3-bromoisoxazoline warhead with a specific peptidomimetic recognition moiety. All derivatives behaved as inhibitors of rhodesain, with low micromolar Ki values. Their activity against the enzyme was found to be paralleled by an in vitro antitrypanosomal activity, with IC50 values in the mid-micromolar range. Notably, a preference for parasitic over human proteases, specifically cathepsins B and L, was observed.

ProteasesStereochemistryPeptidomimeticCathepsin LMolecular ConformationStereoisomerismCysteine Proteinase InhibitorsBiologyCrystallography X-RayBiochemistryCysteine Proteinase InhibitorsCathepsin BCathepsin LinhibitorsDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticstrypanosomarhodesainPharmacologychemistry.chemical_classificationOrganic ChemistryStereoisomerismIsoxazolesisoxazolinesCombinatorial chemistryIn vitroCysteine EndopeptidasesEnzymechemistrypeptidomimeticsbiology.proteinMolecular Medicineinhibitors; isoxazolines; peptidomimetics; rhodesain; trypanosomaProtein Binding
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Identification of Plakortide E from the Caribbean Sponge Plakortis halichondroides as a Trypanocidal Protease Inhibitor using Bioactivity-Guided Frac…

2014

In this paper, we report new protease inhibitory activity of plakortide E towards cathepsins and cathepsin-like parasitic proteases. We further report on its anti-parasitic activity against Trypanosoma brucei with an IC50 value of 5 mu M and without cytotoxic effects against J774.1 macrophages at 100 mu M concentration. Plakortide E was isolated from the sponge Plakortis halichondroides using enzyme assay-guided fractionation and identified by NMR spectroscopy and mass spectrometry. Furthermore, enzyme kinetic studies confirmed plakortide E as a non-competitive, slowly-binding, reversible inhibitor of rhodesain.

ProteasesStereochemistrymedicine.medical_treatmentTrypanosoma brucei bruceiPlakortis halichondroidesPharmaceutical ScienceTrypanosoma brucei01 natural sciences570 Life sciencesDioxanesprotease inhibitor03 medical and health sciencesddc:593Drug DiscoverymedicineAnimalsHumansProtease Inhibitorscathepsinlcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)IC50030304 developmental biologyTrypanocidal agentrhodesainchemistry.chemical_classification0303 health sciencesProteaseAntiparasitic Agentsbiology010405 organic chemistryCommunicationplakortide Ebiology.organism_classificationCathepsinsTrypanocidal AgentsAntiparasitic agentProtease inhibitor (biology)Porifera0104 chemical sciencesCysteine Endopeptidasesslowly-binding reversible inhibitorEnzymelcsh:Biology (General)BiochemistrychemistryDrug Screening Assays Antitumor570 Biowissenschaftenmedicine.drug
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Resistance toBacillus thuringiensis Cry1Ac toxin in three strains ofHeliothis virescens: Proteolytic and SEM study of the larval midgut

1999

In a previous study, we demonstrated that resistance to Bacillus thuringiensis toxins in Heliothis virescens might be related to differences in the composition of the proteolytic extracts from insect midgut. There, we found specific proteolytic bands present in the gut extracts of the resistant strain and absent from the susceptible one. Here we report related facts using a new resistant strain (KCB) and a cross between the two strains used in our previous study. As would be expected, no quantitative differences in total proteolytic activity were found between the strains, although qualitative differences related to the presence or absence of specific proteolytic activity bands using SDS-PA…

ProteasesStrain (chemistry)Heliothis virescensbiologyPhysiologyToxinmedia_common.quotation_subjectfungiMidgutGeneral MedicineInsectmedicine.disease_causebiology.organism_classificationBiochemistryMicrobiologyCry1AcInsect ScienceBacillus thuringiensismedicinemedia_commonArchives of Insect Biochemistry and Physiology
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Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.

2014

Increased expression of metalloprotease meprin β is associated with fibrotic syndromes and Alzheimer's disease (AD). Hence, regulation of meprin activity might be a suitable strategy for the treatment of these conditions. Meprin β is a type 1 transmembrane protein, but can be released from the cell surface by ectodomain shedding. The protease is expressed as an inactive zymogen and requires proteolytic maturation by tryptic serine proteases. In the present study, we demonstrate, for the first time, the differences in the activation of soluble and membrane bound meprin β and suggest transmembrane serine protease 6 [TMPRSS6 or matriptase-2 (MT2)] as a new potent activator, cleaving off the pr…

ProteasesTMPRSS6Swinemedicine.medical_treatmentMolecular Sequence DataBiologyBiochemistryProtein Structure SecondaryAmyloid beta-Protein PrecursorChlorocebus aethiopsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologySerine proteaseProteaseCell MembraneSerine EndopeptidasesMetalloendopeptidasesCell BiologySheddaseTrypsinTransmembrane proteinHEK293 CellsBiochemistryEctodomainCOS Cellsbiology.proteinmedicine.drugThe Biochemical journal
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Controlling the semi-permeability of protein nanocapsules influences the cellular response to macromolecular payloads.

2021

Nanocapsules are an excellent platform for the delivery of macromolecular payloads such as proteins, nucleic acids or polyprodrugs, since they can both protect the sensitive cargo and target its delivery to the desired site of action. However, the release of macromolecules from nanocapsules remains a challenge due to their restricted diffusion through the nanoshell compared to small molecule cargo. Here, we designed degradable protein nanocapsules with varying crosslinking densities of the nanoshell to control the release of model macromolecules. While the crosslinking did not influence the degradability of the capsules by natural proteases, it significantly affected the release profiles. F…

ProteasesVaccinesChemistryMacromolecular SubstancesBiomedical EngineeringProteinsGeneral ChemistryGeneral MedicineSmall moleculeNanocapsulesNanoshellPermeabilityFluorescamineDrug LiberationDrug Delivery SystemsNanocapsulesPermeability (electromagnetism)Restricted DiffusionBiophysicsGeneral Materials ScienceEndopeptidase KSite of actionMacromoleculeJournal of materials chemistry. B
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