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GDP does not support activation of adenylate cyclase nor ADP‐ribosylation of a guanine nucleotide binding protein by cholera toxin
Author(s) -
Shimada Nobuko,
Kimura Narimichi
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80419-0
Subject(s) - adenylate kinase , cholera toxin , cyclase , adp ribosylation , guanine , adp ribosylation factor , nucleotide , chemistry , toxin , biochemistry , biology , endocrinology , nad+ kinase , enzyme , gene , golgi apparatus , cell
The actions of cholera toxin (i.e., activation of adenylate cyclase and ADP‐ribosylation of a guanine nucleotide binding protein in purified membranes fronm rat liver) were GTP dependent. Neither of these actions of cholera toxin was reproduced with GDP. Simultaneous addition of ATP and MgCl 2 along with GDP allowed cholera toxin to exert these actions. The role of GDP in adenylate cyclase regulation was discussed.