ISSN:
1573-7284
Keywords:
EnterotoxigenicEscherichia coli
;
Yibrio cholerae
;
LT
;
CT
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract It was examined where a protease purified from Vibrio cholerae might nick the heat-labile enterotoxin (LT) A subunit from enterotoxigenicEscherichia coli. LT was digested by the protease and contained a fragment which had the same mobility on SDS-PAGE as that of the Al fragment of LT digested by trypsin. The biological activity of LT by this protease was also identical to that of LT by trypsin. The amino acid sequence of the N-terminus of the A2-like fragment was Thr-Ser-Thr-Gly, which corresponded to the sequence from 193 to 196 of the A subunit. These data suggest that this protease, like trypsin, nicks arginine at position 192 from the N-terminus of the A subunit and that the biological activation of LT by this protease is similar to that by trypsin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00145394
Permalink