Abstract
Recently it was shown that porcine pancreatic phospholipase A2 aggregates in the presence of submicellar concentrations of anionic substrates [van Oort, M.G., Dijkman, R., Hille, J.D.R., & de Haas, G.H. (1985) Biochemistry 24, 7993-7999]. In the resulting complexes the enzyme displays very high catalytic activity. In this study the interaction process was further investigated by using pancreatic phospholipases A2 of different origins and several semisynthetic mutants in which one particular amino acid residue was substituted. By use of directing binding studies with a nondegradable anionic substrate analogue and monomolecular surface film kinetics on 1,2-didecanoyl-sn-glycerol 3-sulfate, it is shown that the aggregation process is controlled by the ionization state of the side chains of the amino acid residues at positions 6 and 17.
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 callDisclaimer: 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.
