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ADP-ribosyltransferase type A from turkey erythrocytes modifies actin at Arg-95 and Arg-372.
Just I, Sehr P, Jung M, van Damme J, Puype M, Vandekerckhove J, Moss J, Aktories K. Just I, et al. Among authors: vandekerckhove j. Biochemistry. 1995 Jan 10;34(1):326-33. doi: 10.1021/bi00001a040. Biochemistry. 1995. PMID: 7819215
In contrast, Clostridium perfringens iota toxin ADP-ribosylates only G-actin, with modification at arginine-177 [Vandekerckhove, J., et al. (1987) FEBS Lett. 255, 48-42]. Transferase A-catalyzed modifications are sensitive to 0.5 M neutral hydroxylamine, consistent …
In contrast, Clostridium perfringens iota toxin ADP-ribosylates only G-actin, with modification at arginine-177 [Vandekerckhove, J …
Protein-chemical analysis of pertussis toxin reveals homology between the subunits S2 and S3, between S1 and the A chains of enterotoxins of Vibrio cholerae and Escherichia coli and identifies S2 as the haptoglobin-binding subunit.
Capiau C, Petre J, Van Damme J, Puype M, Vandekerckhove J. Capiau C, et al. Among authors: vandekerckhove j. FEBS Lett. 1986 Aug 18;204(2):336-40. doi: 10.1016/0014-5793(86)80839-0. FEBS Lett. 1986. PMID: 3525228 Free article.
557 results