General description
RNase A, Ribonuclease A, is an endoribonuclease that cleaves the phosphodiester bonds of single strand RNA after pyrimidine nucleotides. It attacks at the 3′ phosphate end (For example pG-pG-pC-pA-pG will be cleaved to give pG-pG-pCp and A-pG). The highest activity is exhibited with single stranded RNA. RNase A is a single chain polypeptide containing 4 disulfide bridges. In contrast to RNase B, it is not a glycoprotein. Ribonucleases do not hydrolyze DNA, because the DNA lacks 2′-OH groups essential for the formation of cyclic intermediates. RNase A can also hydrolyze RNA from protein samples. RNase A can be inhibited by alkylation of His12 and His119 and activated by potassium and sodium salts. RNAse is inhibited in the presence of heavy metal ions. RNase is also inhibited competitively by DNA.
Application
- RNase A is used to remove RNA from DNA plasmid and genomic DNA preparations and protein samples.
- RNase A is also used in RNA sequence analysis and protection assays.
- RNase A has been used as a tool for computer-aided drug design.
- RNase A supports the analysis of RNA sequences.
- RNase A hydrolyze RNA contained in protein samples.
- Purification of DNA is supported by RNase A.
Features and Benefits
Our highly stable Ribonuclease A, RNase A, is suitable for removal of RNA, RNA sequencing, and DNA purification.
Unit Definition
1 U corresponds to the amount of enzyme which hydrolyzes the RNA at a rate constant k = 1 at 25°C and pH 5.0 (Kunitz-units); M. Kunitz, J. Biol. Chem. 164, 563 (1946)
Analysis Note
Protein determined by E.
Other Notes
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The enzyme only hydrolyzes phosphodiester linkages which originate from pyrimidine-3′-phosphates, as well as a large number of 2′,3′-cyclo compounds of cytidine and uridine derivatives; The return of pancreatic ribonucleases