Abstract
A ribonuclease from 6 day old larvae of Ceratitis capitata has been purified to homogeneity by a four step procedure. The enzyme appears as a single polypeptide chain of approx. 34 kDa. Poly(U) and poly(C) are the only polyribonucleotides degraded under standard assay conditions. The enzyme degrades the mRNA present in polysomes inducing a shift of polysomes to monosomes. However, no major cleavage could be observed in the mRNA and the ribosomal RNA when the incubation with the ribonuclease took place under protein synthesis conditions of polysomes.
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