J. Miller, K. H. Boswell, K. Muneyama
Dec 10, 1973
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0
Influential Citations
13
Citations
Quality indicators
Journal
Biochemical and biophysical research communications
Abstract
Abstract The effect of modifying adenosine 3′,5′-cyclic phosphate in the 7-position was studied by investigating tubercidin-, toyocomycin-, and sangivamycin-3′,5′-cyclic phosphates as activators of adenosine 3′,5′-cyclic phosphate-dependent protein kinases and as substrates for and inhibitors of adenosine 3′,5′-cyclic phosphate phosphodiesterases. The same decreasing order of activity was seen with the cyclic phosphates as kinase activators or phosphodiesterase substrates: tubercidin- > toyocomycin- > sangivamycin-3′,5′-cyclic phosphate. The I50 values of the heterocyclic base, nucleoside, nucleoside 5′-phosphate, and nucleoside 3′,5′-cyclic phosphate of tubercidin, toyocomycin, and sangivamycin were determined for the inhibition of adenosine 3′,5′-cyclic phosphate hydrolysis. The heterocyclic bases and the nucleoside 3′,5′-cyclic phosphates were very good inhibitors while the nucleosides and nucleoside 5′-phosphates were in general quite poor inhibitors.