Dehazya P, Coles R S
J Bacteriol. 1980 Jul;143(1):205-11. doi: 10.1128/jb.143.1.205-211.1980.
Various aspects of agglutination of human erythrocytes by fusobacterium nucleatum were examined. Titration experiments done in buffered saline at pH 6 to 10 showed the same agglutination endpoint. The presence of high concentrations of NaCl in reaction mixtures did not alter titers, but KCl in concentrations of 0.5 to 3.6 M increased titers twofold. The agglutinin was inactivated by heat, acid, alkali, 5% Formalin, and the proteolytic enzyme subtilopeptidase A and therefore appeared to be a protein. Treatment of bacterial cells with 2-mercaptoethanol had no effect. Hemagglutination inhibition experiments revealed that arginine and other compounds containing a guanido group as part of their structure were inhibitory at low concentrations. Various hexoses, some hexose derivatives, and most common metal ions, when added to bacterium-erythrocyte mixtures, had no effect. The binding of dansyl-L-arginine to bacteria, but not erythrocytes, was demonstrable by ultraviolet fluorescence microscopy.
对具核梭杆菌凝集人红细胞的各个方面进行了研究。在pH 6至10的缓冲盐溶液中进行的滴定实验显示出相同的凝集终点。反应混合物中高浓度的NaCl的存在不会改变滴度，但浓度为0.5至3.6 M的KCl会使滴度增加两倍。凝集素被热、酸、碱、5%福尔马林和蛋白水解酶枯草杆菌肽酶A灭活，因此似乎是一种蛋白质。用2-巯基乙醇处理细菌细胞没有效果。血凝抑制实验表明，精氨酸和其他结构中含有胍基的化合物在低浓度时具有抑制作用。当将各种己糖、一些己糖衍生物和最常见的金属离子添加到细菌-红细胞混合物中时，没有效果。通过紫外荧光显微镜可证明丹磺酰-L-精氨酸与细菌而非红细胞的结合。
