Obenauf S D, Fisher R H, Cowman R A, Fitzgerald R J
Infect Immun. 1984 Dec;46(3):797-801. doi: 10.1128/iai.46.3.797-801.1984.
We examined whether the anionic inhibitory proteins identified in mixed saliva from certain caries-free individuals are fragments or degradation products of recognized salivary antimicrobial factors. In the experiments reported here, the anionic inhibitory proteins did not produce precipitin reactions with antisera to any of the established salivary antimicrobial factors examined. Additionally, native, heat-treated, or urea-denatured known salivary antimicrobial factors did not react with the antiserum to the anionic inhibitory proteins. However, the antiserum to the anionic inhibitory proteins was found to be reactive with a protein concentrate from mixed saliva or from separate submandibular and parotid secretions from a number of different donors, as well as with a purified protein fraction containing the homologous anionic inhibitory proteins. These findings suggest that the anionic inhibitory proteins represent intact and unique salivary proteins and not the degradation fragments of salivary antimicrobial protein factors within the oral environment.
我们研究了在某些无龋个体的混合唾液中鉴定出的阴离子抑制蛋白是否是公认的唾液抗菌因子的片段或降解产物。在本文报道的实验中，阴离子抑制蛋白与针对所检测的任何一种既定唾液抗菌因子的抗血清均未产生沉淀反应。此外，天然的、经热处理的或经尿素变性的已知唾液抗菌因子与针对阴离子抑制蛋白的抗血清也不发生反应。然而，发现针对阴离子抑制蛋白的抗血清与来自多个不同供体的混合唾液、或来自单独的下颌下腺和腮腺分泌物的蛋白浓缩物发生反应，也与含有同源阴离子抑制蛋白的纯化蛋白组分发生反应。这些发现表明，阴离子抑制蛋白代表完整且独特的唾液蛋白，而非口腔环境中唾液抗菌蛋白因子的降解片段。
