Stecher B, Weller U, Habermann E, Gratzl M, Ahnert-Hilger G
Abteilung Anatomie und Zellbiologie der Universität Ulm, FRG.
FEBS Lett. 1989 Sep 25;255(2):391-4. doi: 10.1016/0014-5793(89)81129-9.
The heavy and light chains of botulinum A toxin were separated by anion exchange chromatography. Their intracellular actions were studied using bovine adrenal chromaffin cells permeabilized with streptolysin O. Purified light chain inhibited the Ca2+-stimulated [3H]noradrenaline release with a half-maximal effect at about 1.8 nM. The inhibition was incomplete. Heavy chain up to 28 nM was neither effective by itself nor did it enhance the inhibitory effect of light chain. It is concluded that the light chain of botulinum A toxin contains the functional domain responsible for the inhibition of exocytosis.
通过阴离子交换色谱法分离肉毒杆菌A毒素的重链和轻链。使用经链球菌溶血素O通透处理的牛肾上腺嗜铬细胞研究它们的细胞内作用。纯化的轻链抑制Ca2+刺激的[3H]去甲肾上腺素释放,在约1.8 nM时具有半数最大效应。抑制作用不完全。高达28 nM的重链本身无效,也不增强轻链的抑制作用。得出结论,肉毒杆菌A毒素的轻链含有负责抑制胞吐作用的功能域。