Search results for "Pore forming protein"

showing 3 items of 3 documents

Selective permeabilization of infected host cells with pore-forming proteins provides a novel tool to study protein synthesis and viability of the in…

2001

Cell Membrane PermeabilityErythrocytesPlasmodium falciparumProtozoan ProteinsRicinPore forming proteinMicrobiologychemistry.chemical_compoundBacterial ProteinsmedicineProtein biosynthesisAnimalsHumansMalaria FalciparumMolecular BiologybiologyMacrophagesToxoplasma gondiiPlasmodium falciparumbiology.organism_classificationmedicine.diseaseToxoplasmosisCell biologyRicinchemistryStreptolysinsParasitologyStreptolysinToxoplasmaToxoplasmosisIntracellularMolecular and Biochemical Parasitology
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Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O

1996

Plasmodium falciparum is an intracellular parasite of human red blood cells (RBCs). Like many other intracellular parasites, P. falciparum resides and develops within a parasitophorous vacuole which is bound by a membrane that separates the host cell cytoplasm from the parasite surface. Some parasite proteins are secreted into the vacuolar space and others are secreted, by an as yet poorly defined pathway, into the RBC cytosol. The transport of proteins from the parasite has been followed mainly using morphological methods. In search of an experimental system that would allow (i) dissection of the individual steps involved in transport from the parasite surface into the RBC cytosol, and (ii…

Cell Membrane PermeabilityErythrocytesPlasmodium falciparumProtozoan ProteinsVacuoleBiologymedicine.disease_causeBiochemistryPore forming proteinAdenosine TriphosphateCytosolBacterial ProteinsProtein targetingSerinemedicineAnimalsHumansMolecular BiologyIntracellular parasiteErythrocyte Membranehemic and immune systemsIntracellular MembranesCell BiologyCell biologyTransport proteinCytosolBiochemistryStreptolysinsVacuolesHost cell cytoplasmIntracellularcirculatory and respiratory physiologyResearch ArticleSubcellular FractionsBiochemical Journal
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Purification and characterization of a pore-forming protein from the marine sponge Tethya lyncurium

1992

A pore-forming protein was detected and purified for the first time from a marine sponge (Tethya lyncurium). The purified protein has a polypeptide molecular mass of 21 kDa and a pI of 6.4. Tethya pore-forming protein (also called Tethya hemolysin) rapidly lysed erythrocytes from a variety of organisms. After binding to target membranes, the hemolysin resisted elution with EDTA, salt or solutions of low ionic strength and hence resembled an integral membrane protein. Erythrocytes could be protected from hemolysis induced by Tethya hemolysin by addition of 30 mM dextran 4 (4-6 kDa; equivalent hydrodynamic diffusion radius, 1.75-2.3 nm) to the extracellular medium, but not by addition of unch…

Cell Membrane PermeabilityLysisChemical PhenomenaCarbohydratesHemolysisBiochemistryPore forming proteinHemolysin ProteinsAdenosine TriphosphateOsmotic PressureAnimalsHumansColloidsIntegral membrane proteinSheepbiologyMolecular massChemistry PhysicalErythrocyte MembraneDextransHemolysinMembrane transportbiology.organism_classificationPoriferaMolecular WeightMicroscopy ElectronMembraneBiochemistryChromatography GelPotassiumTethyaRabbits
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