Abstract
The sequence of the first 66 amino acids of the amino-terminal part of the enterotoxin from Clostridium perfringens type A is presented. The trypsin activation of the enterotoxin involves hydrolysis of Lys15-Glu16 and Lys25-Thr26 bonds. The N-terminal sequence of the trypsin-activated enterotoxin has limited homology with the sequence of the N-terminal region of the cholera toxin B subunit.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
19 articles.
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