从口腔细菌缓症链球菌ATCC 9811培养基中分离出的神经氨酸酶的纯化及某些特性

Purification and some properties of neuraminidase isolated from the culture medium of oral bacterium Streptococcus mitis ATCC 9811.

作者信息

Nonaka H, Ishikawa Y, Otsuka M, Toda K, Sato M, Nakamura R

出版信息

J Dent Res. 1983 Jul;62(7):792-7. doi: 10.1177/00220345830620070301.

DOI:10.1177/00220345830620070301

Abstract

Neuraminidase acting on the salivary bacterial agglutinating factor was isolated and purified from the culture medium of Streptococcus mitis ATCC 9811. The molecular weight and the isoelectric point of the enzyme were determined to be 42,000 and a pH of 4.6, respectively. The enzyme showed high activity against human glycoprotein substrates, especially the salivary bacterial agglutinating factor.

摘要

从缓症链球菌ATCC 9811的培养基中分离并纯化了作用于唾液细菌凝集因子的神经氨酸酶。该酶的分子量和等电点分别测定为42,000和pH 4.6。该酶对人糖蛋白底物表现出高活性，尤其是唾液细菌凝集因子。