Abstract
SUMMARY: A hyaluronidase preparation was isolated by the methods of protein precipitation from the culture fluid of a capsulated group C streptococcus cultivated in a serum-free medium. The preparation was active in the mucin clot prevention and turbidimetric tests for hyaluronidase and rapidly destroyed the capsules of group A and group C streptococci. The enzyme resembled other streptococcal hyaluronidases in its reaction to pH changes but differed from these both in its thermolability and antigenic specificity.