Abstract
Abstract A ribonuclease has been partially purified from the soluble fraction of rabbit reticulocytes. The enzyme degraded RNA predominantly to oligonucleotides with an average chain length of six. It degraded polycytidylic acid and polyuridylic acid but not polyadenylic acid, polyguanylic acid, or polyinosinic acid. When natural RNA was the substrate, the oligonucleotide product had mainly uridine, guanosine, and some cytidine residues at the 3' end. The 3' terminus had a cyclic 2',3'-phosphodiester bond. The enzyme was capable of degrading polyribosomes. Hemin inhibited reticulocyte RNase. Hemin did not inhibit pancreatic RNase or RNase T1, but did inhibit pea leaf RNase. Both reticulocytes and pea leaves contain metalloporphyrin. An hypothesis is presented for the role of reticulocyte RNase in control of protein synthesis in these cells.
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