Search results for "Blood Protein"

showing 10 items of 175 documents

Zur Permeation der Serumeiwei�e in die Haut und ihrer quantitativen Bestimmung am Modell der Cantharidenblase

1964

Mittels chemischer und immunochemischer Methoden wurde vergleichend der Gehalt an Proteinen in Cantharidenblasen und Blutserum bestimmt. Erstmals werden auch quantitative Untersuchungen von Praalbumin, α2-M-Globulin, Coeruloplasmin, Haptoglobin und Transferrin im Cantharidenblaseninhalt vorgenommen. Dabei fanden sich statistisch gesicherte Unterschiede zwischen Cantharidenblasen- und Seruminhalt im Sinne tieferer Werte in den Blasen bei Gesamteiweis, Praalbumin abs., α2-M-Globulin abs., α2-Globulin abs. und rel.-%, Coeruloplasmin abs., β-Globulin abs., Transferrin abs. und γ-Globulin abs. Albumin abs. und rel.-% wiesen signifikante Unterschiede in Richtung hoherer Werte in den Cantharidenbl…

Cantharidinchemistry.chemical_compoundChemistryDrug DiscoveryMolecular MedicineCantharidesGeneral MedicineBlood proteinsMolecular biologyGenetics (clinical)Klinische Wochenschrift
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Cholinesterase Activity and Hematological Parameters as Biomarkers of Sublethal Molinate Exposure in Anguilla anguilla

2000

Cholinesterase (ChE) activity was measured in plasma, whole blood [using 5,5'-dithiobis(2-nitrobenzoic acid) and 2-PDS as chromophores], brain, and whole eyes of Anguilla anguilla exposed to a sublethal concentration of 11.15 mg/L (one-third of the 96-h LC(50)) of the carbamate herbicide molinate. ChE activity was evaluated after 6, 24, 48, 72, and 96 h of pesticide exposure. Results indicated that ChE activity in eel tissues decreased as time of exposure increased, especially in eel blood. Eels exposed to molinate were transferred to a pesticide-free water for a recovery period of 4 days and ChE activity was also evaluated. Results indicated that ChE activity for those animals with preexpo…

CarbamateHealth Toxicology and Mutagenesismedicine.medical_treatmentPhysiologyHematocritToxicologyThiocarbamatesAnguillidaeBlood plasmamedicineAnimalsCholinesterasesCholinesteraseWhole bloodBlood CellsEelsintegumentary systembiologymedicine.diagnostic_testHerbicidesPublic Health Environmental and Occupational HealthAzepinesBlood ProteinsGeneral Medicinebiology.organism_classificationPollutionBlood proteinsToxicitybiology.proteinCarbamatesCholinesterase InhibitorsBiomarkersEcotoxicology and Environmental Safety
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Fetuin-A and Cystatin C Are Endogenous Inhibitors of Human Meprin Metalloproteases

2010

Meprin α and β, zinc metalloproteinases, play significant roles in inflammation, including inflammatory bowel disease (IBD), possibly by activating cytokines, like interleukin 1β, interleukin 18, or tumor growth factor α. Although a number of potential activators for meprins are known, no endogenous inhibitors have been identified. In this work, we analyzed the inhibitory potential of human plasma and identified bovine fetuin-A as an endogenous meprin inhibitor with a K(i) (inhibition constant) of 4.2 × 10(-5) M for meprin α and a K(i) of 1.1 × 10(-6) M meprin β. This correlated with data obtained for a fetuin-A homologue from carp (nephrosin inhibitor) that revealed a potent meprin α and β…

Carpsalpha-2-HS-GlycoproteinMolecular Sequence DataMatrix metalloproteinaseBiochemistryPlasma03 medical and health sciencesmedicineAnimalsHumansAmino Acid SequenceCystatin C030304 developmental biology0303 health sciencesMetalloproteinasebiology030302 biochemistry & molecular biologyProteolytic enzymesMetalloendopeptidasesBlood ProteinsTrypsinFetuinProtease inhibitor (biology)3. Good healthBiochemistryCystatin Cbiology.proteinCattleCystatinSequence Alignmentmedicine.drugBiochemistry
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Multiple sclerosis patient-derived CSF induces transcriptional changes in proliferating oligodendrocyte progenitors.

2014

Background: Cerebrospinal fluid (CSF) is in contact with brain parenchyma and ventricles, and its composition might influence the cellular physiology of oligodendrocyte progenitor cells (OPCs) thereby contributing to multiple sclerosis (MS) disease pathogenesis. Objective: To identify the transcriptional changes that distinguish the transcriptional response induced in proliferating rat OPCs upon exposure to CSF from primary progressive multiple sclerosis (PPMS) or relapsing remitting multiple sclerosis (RRMS) patients and other neurological controls. Methods: We performed gene microarray analysis of OPCs exposed to CSF from neurological controls, or definitive RRMS or PPMS disease course. R…

Cell physiologyAdultPathologymedicine.medical_specialtyTranscription GeneticGalectin 3GalectinsImmunocytochemistryBiologyArticleCerebrospinal fluidMultiple Sclerosis Relapsing-RemittingNeural Stem CellsmedicineAnimalsHumansProgenitor cellCells CulturedCell ProliferationCerebrospinal FluidMultiple sclerosisBrainHuman brainBlood ProteinsMultiple Sclerosis Chronic Progressivemedicine.diseaseMicroarray AnalysisNeural stem cellOligodendrocyteRatsUp-RegulationOligodendrogliamedicine.anatomical_structureNeurologyNeurology (clinical)Multiple sclerosis (Houndmills, Basingstoke, England)
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Transport of resveratrol, a cancer chemopreventive agent, to cellular targets: plasmatic protein binding and cell uptake

2004

Resveratrol produced by several plants, berries and fruits, including grapes, is one of the best known natural food microcomponents with potent chemopreventive properties towards the most severe contemporary human diseases: cardiovascular sickness, cancer and neurodegenerative pathologies. Demonstration of its mechanism of action also implies the elucidation of the steps of bioavailability and bioabsorption in cells and tissues. In order to estimate the relationships between the amounts of resveratrol taken up by food or drink intake, and the several possible benefits illustrated from in vitro/in vivo experiments and from epidemiological studies, it is essential to demonstrate step by step …

CellPlasma protein bindingPharmacologyResveratrolBiologyBiochemistrychemistry.chemical_compoundIn vivoStilbenesTumor Cells CulturedmedicineAnimalsAnticarcinogenic AgentsHumansAnticarcinogenSerum AlbuminPharmacologyFatty Acidsfood and beveragesBiological TransportBlood ProteinsIn vitromedicine.anatomical_structureBiochemistryMechanism of actionchemistryResveratrolmedicine.symptomIntracellularProtein BindingBiochemical Pharmacology
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�ber den Einbau von14C-Leucin in Kaninchen-Reticulocyten

1965

Es wird uber den Einbau von14C-Leucin in Kaninchen-Reticulocyten berichtet. Die Markierung des Proteins und einer Lipidfraktion aus ganzen Zellen war abhangig von Zeit und Temperatur. Bei Auftrennung von Zellhomogenaten in subcellulare Fraktionen erreichte die Mikrosomenfraktion sehr fruh eine mindestens doppelt so hohe spezifische Aktivitat wie die ubrigen Fraktionen. Erythrocyten von Mensch und Kaninchen bauten markiertes Leucin nicht ein. Weiterhin wird die Basenzusammensetzung der ribosomalen RNA von Kaninchen-Reticulocyten angegeben.

ChemistryDrug DiscoveryMicrosomeMolecular MedicineRNAGeneral MedicineLeucineRibosomeBlood proteinsMolecular biologyGenetics (clinical)Klinische Wochenschrift
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Characterization of antihistamine–human serum protein interactions by capillary electrophoresis

2007

An important topic in the drug discovery and development process is the role of drug binding to plasma proteins. In this paper the characterization of the interaction between antihistamines (cationic drugs) towards human serum albumin (HSA) and alpha(1)-acid glycoprotein (AGP) under physiological conditions by capillary electrophoresis-frontal analysis is presented. Furthermore, the binding of these drugs to all plasma proteins is evaluated by using ultrafiltration and capillary electrophoresis. Antihistamines present a wide-ranging behaviour with respect to their affinities towards plasma proteins. Orphenadrine, phenindamine, tripelenamine and tripolidine principally bind to HSA; carbinoxa…

ChromatographyPhenindamineChemistryOrganic ChemistryElectrophoresis CapillaryBlood ProteinsGeneral MedicinePlasma protein bindingBrompheniramineHuman serum albuminBiochemistryBlood proteinsAnalytical Chemistrychemistry.chemical_compoundChlorcyclizineBiochemistryDimetindeneHistamine H1 AntagonistsmedicineHumansCarbinoxamineProtein Bindingmedicine.drugJournal of Chromatography A
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Infrared biospectroscopy for a fast qualitative evaluation of sample preparation in metabolomics.

2014

Liquid chromatography-mass spectrometry (LC-MS) has been increasingly used in biomedicine to study the dynamic metabolomic responses of biological systems under different physiological or pathological conditions. To obtain an integrated snapshot of the system, metabolomic methods in biomedicine typically analyze biofluids (e.g. plasma) that require clean-up before being injected into LC-MS systems. However, high resolution LC-MS is costly in terms of resources required for sample and data analysis and care must be taken to prevent chemical (e.g. ion suppression) or statistical artifacts. Because of that, the effect of sample preparation on the metabolomic profile during metabolomic method d…

ChromatographyPlasma samplesChemistryPlasma compositionIon suppression in liquid chromatography–mass spectrometryBlood ProteinsMass spectrometryMethod developmentMass SpectrometryAnalytical ChemistryMice Inbred C57BLExploratory data analysisMetabolomicsSpectroscopy Fourier Transform InfraredAnimalsMetabolomicsSample preparationFemaleChromatography LiquidTalanta
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Application of Liquid-Liquid Partition Chromatography (LLPC) in the Preparation of Steroid Binding Proteins

1989

Two human serum proteins, i.e. sex hormone binding globulin (h-SHBG) and corticosteroid binding globulin (h-CBG), rat corticosteroid binding globulin (r-CBG), and progesterone binding globulin (PBG) from new guinea pig were purified by the application of three different modes of chromatography. The proteins were purified by affinity chromatography and anion exchange chromatography. Fractions containing the steroid binding proteins were finally purified by liquid-liquid partition chromatography on LiParGel 750 (Merck, Darmstadt, FRG). This Chromatographic sequence clearly separated the steroid binding proteins from other proteins, mainly from serum albumin without a loss of protein and compl…

ChromatographybiologyChemistrymedicine.medical_treatmentSerum albuminProgesterone-Binding GlobulinDNA-binding proteinBlood proteinsSteroidSex hormone-binding globulinTranscortinAffinity chromatographybiology.proteinmedicine
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Versuche zur fraktionierung von proteingemischen mit polyacrylsäuren

1953

Proteine lassen sich quantitativ aus wasriger saurer Losung durch Polyacrylsauren (P 200–400) ausfallen. Die Symplexe losen sich bei neutralem PH; nach Entfernung der hochpolymeren Saure als schwerlosliches Ba- oder Protaminsalz werden die Proteine undenaturiert zuruckerhalten. Untersucht wurde die Abhangigkeit der ausgefallten Protein-menge vom PH und von der zugesetzten Menge an PAcs bei reinem Serum-Albumin und Globulin (Rind), sowie an Gemischen aus beiden und an Humanserum. Unter Verwendung der Papierelektrophorese konnte die bei allmahlicher Zugabe des Fallungsmittels bei PH 4, 6 eintretende Fraktionierung verfolgt werden, bei der zuerst Albumin, dann die Globuline zur Abscheidung gel…

ChromatographybiologyGlobulinChemistryPolymer chemistrybiology.proteinAlbuminBovine serum albuminNeutral phBlood proteinsDie Makromolekulare Chemie
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