dc.creatorFigueirêdo, P M S
dc.creatorCatani, C F
dc.creatorYano, T
dc.date2003-Nov
dc.date2015-11-27T12:52:31Z
dc.date2015-11-27T12:52:31Z
dc.date.accessioned2018-03-29T00:58:11Z
dc.date.available2018-03-29T00:58:11Z
dc.identifierBrazilian Journal Of Medical And Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas / Sociedade Brasileira De Biofísica ... [et Al.]. v. 36, n. 11, p. 1495-9, 2003-Nov.
dc.identifier0100-879X
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/14576905
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195574
dc.identifier14576905
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295807
dc.descriptionEnterohemolysin produced by Escherichia coli associated with infant diarrhea showed characteristics similar to those of thiol-activated hemolysins produced by Gram-positive bacteria, including inactivation by cholesterol, lytic activity towards eukaryotic cells and thermoinstability. However, enterohemolysin activity was not inactivated by oxidation or by SH group-blocking agents (1 mM HgCl2, 1 mM iodoacetic acid) and the hemolysin (100 microg/ml) was not lethal to mice, in contrast to the lethality of the thiol-activated hemolysin family to animals. Earlier reports showed that intravenous injection of partially purified streptolysin O preparations (0.2 microg) was rapidly lethal to mice. These results suggest that E. coli enterohemolysin is not a thiol-activated hemolysin, despite its ability to bind cholesterol, probably due to the absence of free thiol-group(s) that characterize the active form of the thiol-activated hemolysin molecule.
dc.description36
dc.description1495-9
dc.languageeng
dc.relationBrazilian Journal Of Medical And Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas / Sociedade Brasileira De Biofísica ... [et Al.]
dc.relationBraz. J. Med. Biol. Res.
dc.rightsaberto
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectBacterial Toxins
dc.subjectCell Membrane
dc.subjectCholesterol
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectErythrocytes
dc.subjectEscherichia Coli
dc.subjectEscherichia Coli Proteins
dc.subjectEukaryotic Cells
dc.subjectHemolysin Proteins
dc.subjectHemolysis
dc.subjectMale
dc.subjectMice
dc.subjectProtein Binding
dc.titleThiol-independent Activity Of A Cholesterol-binding Enterohemolysin Produced By Enteropathogenic Escherichia Coli.
dc.typeArtículos de revistas


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