An improved method is described for preparing the enzyme which hydrolyzes the polysaccharide acid contained in vitreous humor, umbilical cord, synovial fluid, and the mucoid phase of group A hemolytic streptococci.
Preparations have been obtained from pneumococci, group A hemolytic streptococci, Clostridium welchii, and from splenic tissue, which display the same specific activity.
Evidence is presented to show that the hydrolytic enzyme is not the same as that responsible for the lysis of pneumococci.
In pneumococci and hemolytic streptococci the major portion of the enzyme is bound to the cell structure. The enzyme from Clostridium welchii is associated with other carbohydrate-splitting enzymes in the culture medium and not with the bacterial cells.
It is suggested that the disappearance of the mucoid capsule of group A hemolytic streptococci is due to enzymatic hydrolysis of the acid polysaccharide.
The relation between enzyme activity and the virulence and invasiveness of group A hemolytic streptococci is briefly considered.