MECHANISM OF ACTIVATION OF ADENYLATE-CYCLASE INVITRO BY POLYMYXIN-RELEASED, HEAT-LABILE ENTEROTOXIN OF ESCHERICHIA-COLI
MECHANISM OF ACTIVATION OF ADENYLATE-CYCLASE INVITRO BY POLYMYXIN-RELEASED, HEAT-LABILE ENTEROTOXIN OF ESCHERICHIA-COLI
复制标题
DOI：
10.1093/infdis/133.supplement_1.s103
复制
发表时间：
1976-01-01
影响因子：
6.4
通讯作者：
EVANS, DG
中科院分区：
文献类型：
--
作者：
GILL, DM;EVANS, DJ;EVANS, DG
大肠杆菌多粘菌素B释放的热不稳定的肠毒性物质以时间和浓度依赖的方式激活鸽子红细胞鬼腺苷酸环化酶。激活需要烟酰胺腺嘌呤二核苷酸、三磷酸腺苷和红细胞上清的另一组分。活性菌的分子量约为23,000-24,000道尔顿，受霍乱弧菌毒素抗体的抑制，并且不会被十二烷基硫酸钠不可逆地变性。因此，在许多方面，来自me的活跃物种。大肠杆菌的行为与霍乱毒素的缩氨酸Al相同。
Heat-labile enterotoxic material released fromEscherichia coliby polymyxin B activates the adenylate cyclase of pigeon erythrocyte ghosts in a time- and concentration- dependent manner. The activation requires nicotinamide adenine dinucleotide, adenosine triphosphate, and another component of the erythrocyte supernatant. The active species has a molecular weight of about 23,000–24,000 daltons, is inhibited by antibodies to the toxin ofVibrio cholerae, and is not irreversibly denatured by sodium dodecyl sulfate. Thus in many respects the active species fromE. colibehaves the same as peptide Al of cholera toxin.