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The light chain but not the heavy chain of botulinum A toxin inhibits exocytosis from permeabilized adrenal chromaffin cells
Author(s) -
Stecher B.,
Weller U.,
Habermann E.,
Gratzl M.,
Ahnert-Hilger G.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81129-9
Subject(s) - exocytosis , chromaffin cell , immunoglobulin light chain , toxin , chemistry , chain (unit) , microbiology and biotechnology , biophysics , secretion , adrenal medulla , biochemistry , biology , endocrinology , immunology , catecholamine , physics , antibody , astronomy
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 Ca 2+ ‐stimulated [ 3 H]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.