Naka A, Iida T, Ohara T, Yamamoto K, Miwatani T, Honda T
Department of Bacterial Infections, Research Institute for Microbial Diseases, Osaka University, Suita, Japan.
Toxicon. 1998 Jul;36(7):1001-5. doi: 10.1016/s0041-0101(97)00135-9.
We analyzed the nicking site of the A subunit of Escherichia coli heat-labile enterotoxin for hemagglutinin/protease produced by Vibrio cholerae non-O1 (NAG-HA/P). The determined nicking site was the Thr193-Ile194 junction, which was distinct from that for a protease of V. cholerae (Ichinose et al., European Journal of Epidemiology 8, 743-747, 1992). We further analyzed proteolytic cleavage by NAG-HA/P of a synthetic peptide corresponding to the nicking region of cholera toxin A subunit and determined the cleavage site to be preferentially between Ser194 and Met195, and in addition between Ser193 and Ser194.
我们分析了霍乱弧菌非O1型(NAG-HA/P)产生的血凝素/蛋白酶对大肠杆菌不耐热肠毒素A亚基的切割位点。所确定的切割位点是苏氨酸193-异亮氨酸194连接处,这与霍乱弧菌一种蛋白酶的切割位点不同(市野濑等人,《欧洲流行病学杂志》8,743 - 747,1992年)。我们进一步分析了NAG-HA/P对与霍乱毒素A亚基切割区域相对应的合成肽的蛋白水解切割情况,确定切割位点优先在丝氨酸194和甲硫氨酸195之间,此外还在丝氨酸193和丝氨酸194之间。