Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
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4. Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity;Shone;Eur J Biochem,1985
5. A 50-kDa fragment from the NH2-terminus of the heavy subunit of Clostridium botulinum type A neurotoxin forms channels in lipid vesicles;Shone;Eur J Biochem,1987
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