Abstract

We previously demonstrated that binding of oleic acid to Cerebratulus lacteus cytolysin A-III results in aggregation of this monomeric protein to a tetramer, concomitant with an increase in hemolytic activity. In the present study, incubation of cytolysin A-III with [ 14C]-oleic acid in the presence of a water-soluble carbodiimide results in covalent incorporation of a maximum of two molecules of the fatty acid into the protein. Labeling is restricted to two large tryptic peptides. Sequence analysis of peptide mixtures derived from the labeled protein reveals that the predominant sites of labeling are Lys-31 and Lys-71; the latter site is part of the C-terminal amphipathic helix previously shown to be important for hemolytic activity while the former lies in the other significant hydrophobic region of this largely hydrophilic protein.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.