-transparent.png){kind=logo}
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.
Related Publications
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
September 1989,
Journal of neurochemistry,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
June 1989,
The Journal of biological chemistry,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
December 1993,
FEBS letters,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
January 1986,
Nature,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
December 1987,
The Journal of biological chemistry,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
January 1989,
FEBS letters,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
February 1996,
Journal of neurochemistry,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
August 1985,
The Physiologist,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
September 1988,
Cellular and molecular neurobiology,
B Stecher, and
U Weller, and
E Habermann, and
M Gratzl, and
G Ahnert-Hilger
May 1989,
FEBS letters,
