Ribonuclease A

Pancreatic Ribonuclease (RNase I) catalyzes cleavage of the phosphodiester bond between the 5'-ribose of a nucleotide and the phosphate group attached to the 3'-ribose of an adjacent pyrimidine nucleotide forming a 2',3'-cyclic phosphate which may then be hydrolyzed to the corresponding 3'-nucleoside phosphate. Ribonuclease A has a molecular weight of 13,700 daltons. It operates in an optimum pH range of 7.0-7.5. Linzyme ultrapure Pancreatic Ribonuclease has been further purified by affinity chromatography method to remove trace contaminating proteases.

Pancreatic Ribonuclease (RNase I) catalyzes cleavage of the phosphodiester bond