In order to devise a method for rapid and facile measurement of lecithinase-A activity, examinations were made on (1) method for preparation of diluted blood suspension for measurement of the enzyme activity, (2) relationship between the amount of lysolecithin and degree of hemolysis, (3) conditions for the formation of lysolecithin, and (4) optimal conditions for enzyme-substrate reaction. Based on these experimental results, a method was devised whereby the activity of lecithinase is calculated from changes of extinction coefficient measured during addition of the reaction mixture of lecithinase-A and egg-yolk lecithin to diluted blood suspension. This method is more sensitive than the existing method which observes the degree of complete hemolysis and the sample required is very small in quantity. This method is also convenient for measuring activity of each fraction during purification through chromatography.