Fukui Y, Fukui K, Moriyama T
Infect Immun. 1973 Sep;8(3):329-34. doi: 10.1128/iai.8.3.329-334.1973.
Whole saliva specimens from eight healthy human adults were examined for neuraminidase. The presence of two types of neuraminidase in four samples out of eight was demonstrated by means of polyacrylamide gel electrophoresis and sucrose density gradient centrifugation. One type is soluble and the other an insoluble, perhaps particle-bound, enzyme. The pH optima were 5.8 for the former and 5.0 to 5.3 for the latter. However, the soluble enzyme could not be detected in the other four saliva specimens which showed low activity. A comparative study of the salivary and other neuraminidases was carried out. It was found that both salivary neuraminidases were closely similar to the enzymes in submandibular-sublingual secretions and in human liver, but not to the oral streptococcal enzymes. The results suggest that the salivary neuraminidases might originate from cells such as epithelial cells or polymorphonuclear leukocytes, or both, in the oral cavity.
对八名健康成年人类的全唾液样本进行了神经氨酸酶检测。通过聚丙烯酰胺凝胶电泳和蔗糖密度梯度离心法，在八个样本中的四个样本中证实了两种类型神经氨酸酶的存在。一种类型是可溶性的，另一种是不溶性的，可能是与颗粒结合的酶。前者的最适pH值为5.8，后者为5.0至5.3。然而，在其他四个活性较低的唾液样本中未检测到可溶性酶。对唾液神经氨酸酶和其他神经氨酸酶进行了比较研究。发现两种唾液神经氨酸酶与下颌下腺-舌下腺分泌物和人肝脏中的酶非常相似，但与口腔链球菌酶不同。结果表明，唾液神经氨酸酶可能起源于口腔中的上皮细胞或多形核白细胞等细胞，或两者皆有。
