dc.creator | Figueirêdo, P M S | |
dc.creator | Catani, C F | |
dc.creator | Yano, T | |
dc.date | 2003-Nov | |
dc.date | 2015-11-27T12:52:31Z | |
dc.date | 2015-11-27T12:52:31Z | |
dc.date.accessioned | 2018-03-29T00:58:11Z | |
dc.date.available | 2018-03-29T00:58:11Z | |
dc.identifier | Brazilian 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.identifier | 0100-879X | |
dc.identifier | | |
dc.identifier | http://www.ncbi.nlm.nih.gov/pubmed/14576905 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/195574 | |
dc.identifier | 14576905 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1295807 | |
dc.description | Enterohemolysin 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.description | 36 | |
dc.description | 1495-9 | |
dc.language | eng | |
dc.relation | Brazilian Journal Of Medical And Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas / Sociedade Brasileira De Biofísica ... [et Al.] | |
dc.relation | Braz. J. Med. Biol. Res. | |
dc.rights | aberto | |
dc.rights | | |
dc.source | PubMed | |
dc.subject | Animals | |
dc.subject | Bacterial Toxins | |
dc.subject | Cell Membrane | |
dc.subject | Cholesterol | |
dc.subject | Electrophoresis, Polyacrylamide Gel | |
dc.subject | Erythrocytes | |
dc.subject | Escherichia Coli | |
dc.subject | Escherichia Coli Proteins | |
dc.subject | Eukaryotic Cells | |
dc.subject | Hemolysin Proteins | |
dc.subject | Hemolysis | |
dc.subject | Male | |
dc.subject | Mice | |
dc.subject | Protein Binding | |
dc.title | Thiol-independent Activity Of A Cholesterol-binding Enterohemolysin Produced By Enteropathogenic Escherichia Coli. | |
dc.type | Artículos de revistas | |