Nishikata M, Yoshimura F, Nodasaka Y
Central Research Division, School of Dentistry, Hokkaido University.
Microbiol Immunol. 1989;33(1):75-80. doi: 10.1111/j.1348-0421.1989.tb01499.x.
Inhibition of hemagglutinin (HA) activity in a membrane fraction of Bacteroides gingivalis was examined using various compounds. Leupeptin and anti-pain inhibited the HA activity at nM order. This potency was lost when the aldehyde group of leupeptin was converted to an alcohol moiety. Irreversible protease inhibitors, tosyl-L-lysine chloromethyl ketone (TLCK), p-chloromercuribenzoate (PCMB), and N-ethylmaleimide (NEM) were also inhibitory. From the inhibition experiments, we speculate that the HA possesses protease activity and that the same site of the molecule participates in the erythrocyte binding and the substrate binding.
使用各种化合物检测了牙龈卟啉单胞菌膜组分中血凝素（HA）活性的抑制情况。亮抑蛋白酶肽和抗痛素在纳摩尔水平抑制HA活性。当亮抑蛋白酶肽的醛基转化为醇部分时，这种效力丧失。不可逆蛋白酶抑制剂甲苯磺酰-L-赖氨酸氯甲基酮（TLCK）、对氯汞苯甲酸（PCMB）和N-乙基马来酰亚胺（NEM）也具有抑制作用。从抑制实验中，我们推测HA具有蛋白酶活性，并且该分子的同一部位参与红细胞结合和底物结合。
