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The hemolysin produced by group C streptococci (GCH) has an isoelectric point (pI) of 5.6 and a molecular weight of 32,000 and shows hemolytic activity in the absence of 2-mercaptoethanol (2-ME). The hemolytic activity of GCH was compared to that of streptolysin S (SLS). These hemolysins did not differ with respect to the binding and release of hemoglobin (Hb). GCH was bound to phospholipids on the membranes of target erythrocytes, followed by the rapid released of K+ and slow Hb release after a relatively long lag time. GCH showed a lower hemolytic efficiency than SLS, reflecting the fact that these hemolysins destroy erythrocytes by slightly different mechanisms.

Properties of a Hemolysin Produced by Group C Streptococci Isolated from Hemolytic Streptococcal Infection in Formosan Squirrels