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Updated: Jul 11, 2026

A Tandem Liquid Chromatography–Mass Spectrometry-based Approach for Metabolite Analysis of Staphylococcus aureus
Published on: March 28, 2017
Correlations between differences in amino-terminal sequences and different hemolytic activity of sticholysins
Eduardo M Cilli1, Fábio T Pigossi, Edson Crusca
1Department of Biochemistry and Technological Chemistry, Institute of Chemistry, UNESP--São Paulo State University, SP, Brazil.
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.

