In this report we describe the partial purification and characterization of an acid ribonuclease from beef brain nuclei (RNAase BN2). RNAase BN2 was purified approximately 85-fold. The optimum pH is 6.2 and the optimum temperature 55°C. The effect of ions on the RNAase BN2 and its K , were determined. RNAase BN2 is an endoribonuclease capable of hydrolysing polyA, polyU and polyC. Oligonucleotides produced by the hydrolysis of polyA by the RNAase BN2 have a monophosphate group at the 3' position.IT IS we11 known that Hn-RNA and pre-rRNA undergo a process of maturation in mammalian nuclei (PERRY, 1967;MADEN, 1970; WEINEIERG, 1973; DAR-NELL et al., 1973), involving partial degradation and cleavage of polynucleotide chains. There is some evidence that nuclear ribonucleases are involved in these phenomena (LIAU et al.
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