Sakamoto N, Nakajima T, Ikunaga K, Shidahara H, Okamoto H, Okuda K
J Dent Res. 1981 Apr;60(4):850-4. doi: 10.1177/00220345810600041601.
A hyaluronidase activity was demonstrated in rabbit dental pulp. The optimum pH of the enzyme was 3.8. The enzyme activity was enhanced by protamine and poly-L-lysine and was inhibited by iodoacetamide, ferric ion, and ferrous ion in decreasing order. The product of the enzyme reaction was identified as tetrasaccharide. From these results it was concluded that the enzyme exists in pulp tissue and is functioning for degradation of proteoglycans in situ.
在兔牙髓中证实存在透明质酸酶活性。该酶的最适pH值为3.8。鱼精蛋白和聚-L-赖氨酸可增强该酶的活性，而碘乙酰胺、铁离子和亚铁离子则依次抑制该酶的活性。酶反应产物被鉴定为四糖。从这些结果可以得出结论，该酶存在于牙髓组织中，并在原位发挥降解蛋白聚糖的作用。
