ADP-Ribosyl Proteins Formed by Pertussis Toxin are Specifically Cleaved by Mercury Ions
1988; De Gruyter; Volume: 369; Issue: 2 Linguagem: Inglês
10.1515/bchm3.1988.369.2.579
ISSN0177-3593
AutoresThomas F. Meyer, Robert Koch, Werner Fanick, Helmuth Hilz,
Tópico(s)Ion channel regulation and function
ResumoVarious types of ADP-ribosyl protein conjugates were synthesized and their chemical stability was compared with that of cysteine-linked ADP-ribosyl groups as formed by incubation of transducin or Gi/Go proteins with NAD and pertussis toxin. Treatment with 0.1 mM HgCl2 specifically cleaved the cysteine-linked conjugates. This may provide a tool for the quantitation of modified Gi/Go proteins as well as of other acceptors modified by ADP-ribose at cysteine residues in the presence of other ADP-ribosyl proteins.
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