ANTI-ENZYME IMMUNITY 237 



Madinaveita and Stacey (1944) studied the effect of testicular 

 hyaluronidase on carbohydrates from various sources. It acted on 

 hyaluronic acid, closely related polysaccharides from placenta and 

 tumor mucin and lowered the viscosity of chondroitin sulfate from 

 nasal septa. The enzyme showed no activity when tested with the fol- 

 lowing polysaccharides as substrates: Blood Group A polysaccharides 

 from both gastric mucin and from pepsin, the latter containing units 

 of 1-fucose, mannose, galactose and N-acetylglucosamine; a galactan 

 from the pancreas; ovomucoid, containing units of N-acetylgluco- 

 samine, mannose and galactose united in a complicated branched chain 

 structure; dextran from L. dextranicum which contains long chains of 

 glucose units linked through the 1- and 6- positions; the Rhizohium 

 radicicolum polysaccharide containing units of glucuronic acid and 

 glucose linked in a manner generally similar to type III pneumococcus 

 polysaccharide; luteose from P. luteum Zukal, a '/S-dextran' constituted 

 solely of units of glucose linked through the 1- and 6- positions; and 

 Azotohacter polysaccharide containing units of glucuronic acid and 

 glucose; and the B. megatherium levan which is built up from units of 

 fructose linked through the 2- and 6- positions. 



3. Mechanism of the Action of Hyaluronidase 



Despite intensive studies carried out during the last decade, 

 hyaluronidases obtained from different sources are still considered 

 mixtures of enzymes. Their specific hydrolytic action still is not clearly 

 defined. According to Rogers (1946), hyaluronidases of CI. welchii, 

 streptococci and bull testes liberate from hyaluronate units of different 

 average sizes with various reducing capacities. Streptococcal enzyme, 

 for example, releases freely diffusible reducing sugar and leaves no re- 

 ducing polysaccharides, whereas testicular hyaluronidase leaves non- 

 diffusible units which account for as much as 20 per cent of the 

 liberated reducing sugar. Hahn (1945, 1946) reported that at pH 4.6 

 one testicular enzyme degraded hyaluronate to freely diffusible disac- 

 charides while a second completed hydrolysis to monosaccharides. 

 These findings indicate that each preparation of hyaluronidase is a 

 mixture of enzymes responsible for various stages of the hydrolysis of 

 the hyaluronate. Hahn (1945) reported likewise that at pH 4.6 

 CI. welchii hyaluronidase preparations do not degrade the polysac- 



