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Corticotropin acth inhibits the binding of b 50 gap 43 to calmodulin



Corticotropin acth inhibits the binding of b 50 gap 43 to calmodulin



Neuroscience Research Communications 6(2): 105-110



Modulation of B-50/GAP-43 binding to calmodulin by corticotropin (ACTH) was investigated, in vitro, using purified dephosphorylated B-50 and calmodulin covalently attached to Sepharose. ACTH1-24 inhibited B-50 binding to calmodulin in a concentration dependent manner (IC50 5.mu.M). ACTH11-24 (50.mu.M) produced a small but significant inhibition whereas ACTH1-10 (50.mu.M) and a synthetic peptide (B-5038-51) spanning the proposed calmodulin binding domain of B-50 were both without effect. Calmodulin is capable of binding several small peptides including ACTH, with affinities in the low micromolar range. Therefore it appears that displacement of B-50 by ACTH may reflect competition for the same binding site on calmodulin.

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