Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins

dc.contributorUniv La Habana
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T15:20:33Z
dc.date.accessioned2022-10-05T16:06:09Z
dc.date.available2014-05-20T15:20:33Z
dc.date.available2022-10-05T16:06:09Z
dc.date.created2014-05-20T15:20:33Z
dc.date.issued2007-12-15
dc.identifierToxicon. Oxford: Pergamon-Elsevier B.V., v. 50, n. 8, p. 1201-1204, 2007.
dc.identifier0041-0101
dc.identifierhttp://hdl.handle.net/11449/31826
dc.identifier10.1016/j.toxicon.2007.07.013
dc.identifierWOS:000251557900017
dc.identifier9424346762460416
dc.identifier0000-0002-4767-0904
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3904505
dc.description.abstractSticholysins I and II (St I and St II) are cytolysins produced by the sea anemone Stichodactyla helianthus. In spite of their 93% sequence homology, St II is more hemolytic against human erythrocytes than St 1. In order to establish the possible causes of this difference, we studied the hemolytic activity of synthetic peptides containing sequences from the N-termini of both proteins. The results demonstrated that the differences in hemolytic activity of the toxins could be ascribed at least partly to differences in their N-termini. (c) 2007 Elsevier Ltd. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationToxicon
dc.relation2.352
dc.relation0,692
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectsticholysin
dc.subjectpeptides
dc.subjecthemolytic activity
dc.subjectsea anemone
dc.titleCorrelations between differences in amino-terminal sequences and different hemolytic activity of sticholysins
dc.typeArtigo


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