Limited Proteolysis of Tetanus Toxin Light Chain by Trypsin at Its C-Terminus Causes a 10–30-Fold Decrease of Activity as Measured by Inhibition of Noradrenaline Release from Permeabilized Chromaffin Cells

  • Dagmar Sanders
  • Jasminka Godowac-Zimmermann
  • Ernst Habermann
  • Ulrich Weller

Abstract

The light chain (L) of tetanus toxin (TeTx) was shown to be the active principle of the inhibitory action of tetanus toxin in permeabilized cell systems, l,2 and if injected into neurons from Aplysia californica.3 It was shown to have the same activity as native toxin on a molar basis.1,3 Different L constructs expressed in E. coli and purified to homogeneity turned out to be proteolytically shortened at the C-terminus. Their activity in digitonin permeabilized chromaffin cells (PCC) was reduced to about 10% as compared with L from native toxin. CYS 438 was essential for activity in vivo but not in PCC.4

Keywords

Light Chain Limited Proteolysis Botulinum Neurotoxin Tetanus Toxin Native Toxin 
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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Dagmar Sanders
    • 1
  • Jasminka Godowac-Zimmermann
    • 2
  • Ernst Habermann
    • 1
  • Ulrich Weller
    • 3
  1. 1.RBI f. PharmakologieJLUGießenFed. Rep. of Germany
  2. 2.Inst. f. Physiologische Chemie u. PathobiochemieJOGUMainzFed. Rep. of Germany
  3. 3.Inst. f. Med. MikrobiologieJOGUMainzFed. Rep. of Germany

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