RNase A is an endoribonuclease that specifically degrades single-stranded RNA
at C and U residues. It cleaves the phosphodiester bond between the 5'-ribose
of a nucleotide and the phosphate group attached to the 3'-ribose of an adjacent
pyrimidine nucleotide. The resulting 2',3'-cyclic phosphate is hydrolyzed to
the corresponding 3'-nucleoside phosphate. The highest activity is exhibited
with single-stranded RNA. RNase A is a single chain polypeptide containing
4 disulfide bridges.
A major application for RNase A is the removal of RNA from preparations of
plasmid DNA. The enzyme is active under a wide range of reaction conditions.
At low salt concentrations (0 to 100 mM NaCl), RNase A cleaves single-stranded
and double-stranded RNA as well as the RN A strand in RNA-DNA hybrids.
However, at NaCl concentrations of 0.3 M or higher, RNase A specifically cleaves
RNase A Solution is a highly purified preparation of recombinant RNase A from
yeast cells with a cloned gene encoding genetically engineered bovine pancreatic
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