Adenosine 3′,5′-Cyclic Monophosphate-Binding Proteins from Trypanosoma gambiense

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Abstract
Two cyclic[c]AMP-binding proteins, not identical with regulatory subunits of protein kinases, were isolated from T. gambiense. The cAMP receptors were separated by gel chromatography on the basis of their MW. The binding constants of the high and the low MW receptors for cAMP were 0.4 .mu.M and 0.6 .mu.M, respectively. cIMP and cGMP competed with cAMP for the binding sites of both receptors. The cAMP binding of the low MW receptor was competitively inhibited by adenine derivatives. The binding capacity of the high MW receptor was enhanced about 2-fold by proteolytic modification with trypsin.

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