Impero J E, Harrison G M, Nelson T E
Pediatr Res. 1978 Feb;12(2):108-14. doi: 10.1203/00006450-197802000-00009.
A ciliostatic factor has been isolated from cystic fibrosis (CF) saliva by dialyzing it from purified alpha-amylase prepared by a glycogen-complex method. This method of isolating the CF factor is an improvement over the previously employed heparin procedure. The activity of the isolated factor is proportional with concentration using the oyster gill ciliostatic assay and in its inhibition of mammalian glycogen debranching enzyme. The ciliostatic action of the factor can be reversed by heparin under certain conditions. The type of inhibition of the debranching enzyme by the isolated CF factor indicates that its chemical structure is similar to that observed with hydroxyalkylamines and polyamine metabolites. Physical properties of the isolated factor indicate that it is of low molecular weight and is labile as a function of pH and temperature. At neutral pH the conditions under which it is maintained have a direct effect on the length of time that it is stable.
通过用糖原复合法制备的纯化α-淀粉酶对囊性纤维化（CF）唾液进行透析，已从其中分离出一种纤毛抑制因子。这种分离CF因子的方法是对先前采用的肝素法的改进。使用牡蛎鳃纤毛抑制试验以及该因子对哺乳动物糖原脱支酶的抑制作用，分离出的因子活性与浓度成正比。在某些条件下，肝素可逆转该因子的纤毛抑制作用。分离出的CF因子对脱支酶的抑制类型表明，其化学结构与羟烷基胺和多胺代谢产物相似。分离出的因子的物理性质表明，它分子量低，并且随pH值和温度而不稳定。在中性pH条件下，其保存条件对其稳定时间有直接影响。
