Abstract
Vicia faba root ribonucleases are bound to Cibacron blue F3GA. A Blue dextran-Sepharose column was used to purify RNase A 3, the more abundant enzyme from V. faba root. Using dinucleoside monophosphate as substrates, it appears that this enzyme behaves as a cyclizing phosphotransferase. With high enzyme/substrate ratios on prolonged digestion a partial release of a nucleoside 3′ phosphate occurs. The specificity is relatively high since only the purine-purine phosphodiester linkages out of 16 types of possible links are easily cleaved. When a pyrimidine is involved in the phosphodiester bond, a much slower rate of attack (Py in 5′) or no attack (Py in 3′) was detected.
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