title: Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins.
abstract: Sticholysins 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 I. 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.
authors.affiliation: Department of Biochemistry and Technological Chemistry, Institute of Chemistry, UNESP--São Paulo State University, SP, Brazil.
authors.forename: Eduardo M
authors.initials: EM
authors.lastname: Cilli
authors.forename: Fábio T
authors.initials: FT
authors.lastname: Pigossi
authors.forename: Edson
authors.initials: E
authors.lastname: Crusca
authors.forename: Uris
authors.initials: U
authors.lastname: Ros
authors.forename: Diana
authors.initials: D
authors.lastname: Martinez
authors.forename: Maria E
authors.initials: ME
authors.lastname: Lanio
authors.forename: Carlos
authors.initials: C
authors.lastname: Alvarez
authors.forename: Shirley
authors.initials: S
authors.lastname: Schreier
mesh_terms: D000595:Amino Acid Sequence; D003064:Cnidarian Venoms / Q000737:chemistry* / Q000633:toxicity; D006461:Hemolysis / Q000187:drug effects*; D006801:Humans; D008969:Molecular Sequence Data; D009930:Organic Chemicals / Q000737:chemistry / Q000633:toxicity; D013329:Structure-Activity Relationship