Abstract
With a purified preparation of pneumococcal hemolysin, a sigmoid relationship was found to exist between lysin concentration and hemolytic activity. Hemolysis was inhibited by a high ratio of erythrocytes to lysin, suggesting a multi-hit mechanism of action. Reaction rate decreased rapidly with time, possibly due to competition between ghosts and unlysed erythrocytes for fixation of lysin. The effects of p H and various agents on the processes of lysin adsorption and hemoglobin release were determined. The pneumococcal preparation did not possess nicotinamide adenine dinucleotide glycohydrolase activity.