ribonuclease A

Ribonuclease A (RNase A) is an endoribonuclease enzyme that catalyzes the hydrolysis of phosphodiester bonds in RNA molecules by cleaving at the 3' phosphate of pyrimidine nucleotides[3]. It is a single-chain polypeptide containing 4 disulfide bridges and exhibits highest activity with single-stranded RNA[3]. The enzyme is derived from bovine pancreas and is widely used in molecular biology applications including plasmid purification, genomic DNA isolation, removal of RNA from DNA samples, and diagnostic assay manufacturing[2]. RNase A has shown potential therapeutic applications including **antitumor activity** through its cytotoxic effects on cancer cells, as well as antimicrobial properties including antibacterial, antiviral, and antifungal activities[1]. The enzyme can be inhibited by alkylation of His12 or His119 residues in its active site[3]. Human RNase A family members (RNase 1-8) participate in various physiological and pathological processes including infection control, immune regulation, neurological function, and cardiovascular protection[1].

Other names

RNase Aribonuclease Ipancreatic ribonucleaseribonuclease 3-pyrimidinooligonucleotidohydrolaseribonuclease3-pyrimidinooligonucleotidohydrolaseribonuclease-3-pyrimidinooligonucleotidohydrolaseendoribonuclease I3'-pyrimidino-oligonucleotidohydrolaseribonucleate 3'-pyrimidino-oligonucleotidohydrolase