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RIBONUCLEASE AND RIBONUCLEIC ACID SYNTHESIS

LOWELL E. HOKIN 1 and MABEL R. HOKIN 1

1 Research Institute, The Montreal General Hospital, Montreal

The specific activities of the ribonucleotides in various fractions of complete ribonuclease digests of P32-labelled RNA have been compared. The specific activity of either of the purine nucleotides is essentially the same in the dialysate and in the core. The specific activities of the pyrimidine nucleotides of the dialysate are higher than the specific activities of the corresponding nucleotides in the core. The specific activities of the pyrimidine mononucleotides are higher than those of the corresponding pyrimidine nucleotides bound as polynucleotides; this can account for the higher specific activities of the pyrimidine nucleotides in the dialysate as compared to the core. The specific activities of the pyrimidine nucleotides bound in polynucleotides appear to be the same in core and dialysate. These data show that pyrimidine nucleotides which are esterified through the 5' hydroxyl of their ribose to the secondary phosphoryl group of an adjacent pyrimidine 3' nucleotide are metabolically more labile than pyrimidine nucleotides esterified in a similar manner to adjacent purine 3' nucleotides. Since ribonuclease attacks the former linkage, but not the latter, the data presented here suggest that ribonuclease may play a role in the turnover of RNA.

Submitted on April 16, 1954


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