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JBC, Vol. 254, Issue 13, 5855-5861, Jul, 1979
J. J. Mekalanos, R. J. Collier and W. R. Romig
Cholera toxin containing intact A chain (Mr = 29,000) was isolated, and its
enzymic properties were characterized. The "unnicked" form of the toxin,
produced by a protease-deficient, hypertoxinogenic mutant of Vibrio
cholerae 569B, had greatly reduced activity in catalyzing the
NAD+-glycohydrolase and ADP-ribosyltransferase reactions as compared to the
naturally nicked form commonly isolated. In the latter, the intact A chain
has been cleaved by bacterial proteases to yield disulfide-linked A1 and A2
chains (Mr = 23,000 and 6,000, respectively). Digestion of unnicked toxin
with trypsin or elastase yielded a nicked form similar to or identical with
the naturally nicked toxin, but chymotryptic digestion did not. Disulfide
bond reduction was necessary for expression of enzymic activity by
naturally nicked or trypsin-nicked toxin, or the A1A2 protomer.
Fractionation of thiol-treated, nicked cholera toxin by ion exchange,
molecular exclusion, or affinity chromatography gave results suggesting
that the reduced toxin displays enzymic activity while remaining
structurally intact.
Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulfide bond reduction, and subunit composition
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