Studies on diffusing factors

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Abstract
Hyaluronidase from Clostridium, welchii was not readily inactivated by O2, did not require O2 for its activity and did not produce conditions which would oxidize reduced rosinduline or reduce indophenol during its activity on hyaluronate at pH 7. The presence or absence of Cu had no influence on the activity of hyaluronidase from Clostridium welchii. Hyaluronidase derived either from C. welchii or testis was partially inactivated by KMnO4 and by iodine; this inactivation was not reversed by Na2S2O4. Hyaluronidase derived either from Group A or Group C streptococci was rapidly inactivated at pH 4.6 but was relatively stable at pH 7. This inactivation explained previous reports of the anomalous viscosimetric behavior of streptococcal hyaluronidase.

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