Proceedings of The Biochemical Society

Abstract

Two water-soluble phospholipases have been investigated: (1) the lecithin-splitting activity of Penicillium notatum phospholipase B, and (2) the phospholipase C (cx-toxin) of Clostridium perfringens. The rate of enzymic hydrolysis has been related to the electrokinetic properties of the phospholipid substrate particles. The c-potential of such particles (e.g. lecithin micelles) has been varied by adding amphipathic molecules to the micelles (i.e. longchain bases or acids) while the c-potential of both substrate and enzyme has been changed by introducing polyvalent ions, e.g. Ca2+ or Fe(CN)683-, into