Effect of nucleoside 5′-di- and 5′-tri-phosphates on pancreatic ribonuclease activity |
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| Authors: | W Gamble and Lemuel D Wright |
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| Institution: | Graduate School of Nutrition, Cornell University, Ithaca, N.Y., and Department of Chemistry and Science Research Institute, Oregon State University, Corvallis, Oregon, U.S.A. |
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| Abstract: | 1. ADP, ATP and GDP inhibited the phosphotransferase activity, the release of cyclic nucleotides from RNA, of ribonuclease. No significant inhibition was elicited by pyrimidine 5'-nucleoside diphosphates, CDP and UDP. 2. Inhibition by ADP, AMP, adenosine, adenine, NAD and NADP was insignificant at the concentrations tested. Small inhibition was observed with high concentrations of AMP and only when soluble RNA was the substrate. 3. Inhibition by ADP was found to be ;uncompetitive'. 4. Results seem to indicate that at least for optimum inhibition the polyphosphate of the purine nucleoside is essential. They further suggest that the inhibitor acts by combining with the enzyme only when the enzyme is bound to the substrate. |
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