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Interaction of mastoparan with the low molecular mass GTP‐binding proteins rho/rac
Author(s) -
Koch Gertrud,
Haberman Barbara,
Mohr Christiane,
Just Ingo,
Aktories Klaus
Publication year - 1991
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(91)81315-y
Subject(s) - mastoparan , heterotrimeric g protein , gtp' , g protein , chemistry , gtp binding protein regulators , biochemistry , adp ribosylation , molecular mass , adp ribosylation factor , gtpase , pertussis toxin , microbiology and biotechnology , biology , enzyme , receptor , nad+ kinase , golgi apparatus , cell
Mastoparan, which has been shown to active G proteins [1], inhibits the ADP‐ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half‐maximally and maximally (90%) at 20 and 100 μM concentrations, respectively. Inhibition of ADP‐ribosylation was enhanced by GTP‐γS. Mastoparan increased GTP hydrolysis by porcine brain rho protein and stimulated GTP binding in a concentration dependent manner. The data suggest that mastoparan not only interacts with heterotrimeric G proteins but also with low molecular mass GTP‐binding proteins of the rho/rac family.