Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin.
نویسندگان
چکیده
Transducin was [32P]ADP-ribosylated by cholera toxin in bovine retinal rod outer segments and then partially purified on omega-amino octyl agarose to remove other ADP-ribosylated proteins. Trypsin digestion of the ADP-ribosylated transducin and further purification using boronate-polyacrylamide beads and high performance liquid chromatography yielded a single radiolabeled tetrapeptide, Ser-Arg-Val-Lys. The ADP-ribose is linked to the guanidinium group of arginine.
منابع مشابه
ADP-ribosylation of transducin by pertussis toxin blocks the light-stimulated hydrolysis of GTP and cGMP in retinal photoreceptors.
Cholera toxin and pertussis toxin catalyze ADP-ribosylation of the alpha-subunits of the GTP-binding stimulatory (Ns) and inhibitory (Ni) coupling components, respectively, of adenylate cyclase. Cholera toxin also catalyzes the ADP-ribosylation of transducin, the GTP-binding signal-coupling protein of retinal rod outer segments, and thereby reduces its light-stimulated GTPase activity. We show ...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 259 2 شماره
صفحات -
تاریخ انتشار 1984