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Related to RNase: RNase P, RNase H


A group of enzymes, widely distributed in nature, which catalyze hydrolysis of the internucleotide phosphodiester bonds in ribonucleic acid (RNA). The sites of hydrolysis may vary considerably, depending upon the specificity of the particular enzyme. Differences in specificity for the site of cleavage have led to the use of these various ribonucleases as tools in determining the structure and chemistry of RNA. See Enzyme, Nucleic acid

Research on ribonuclease has played a prime role in advancing the understanding of protein structure and function; also, it was the first protein to be totally synthesized from its component amino acids. Since the elucidation of the amino acid sequence of ribonuclease, much information has been compiled with regard to the three-dimensional structure of the enzyme and to specific regions of the molecule which are catalytically important. See Protein



an enzyme that depolymerizes ribonucleic acids and synthetic ribonucleotides by breaking the phosphodiester bonds of polynucleotide chains. Ribonucleases exhibit a high specificity in relation to the bases contained in nucleotides; the bonds between different nucleotides are hydrolyzed by different ribonucleases.

Pancreatic ribonuclease secreted by the pancreas of a bull was the first enzyme for which the primary structure, that is, the sequence of amino acids, was fully established (1960–62). The polypeptide chain of this enzyme consists of 124 amino-acid residues and contains four disulfide bridges that stabilize the enzyme’s spatial configuration. Pancreatic ribonuclease was first chemically synthesized in 1969.

In biochemical research ribonucleases are used in establishing the sequence of nucleotides in RNA, and in medicine they are used in treating certain viral diseases.


Khimiia biologicheski aktivnykh prirodnykh soedinenii. Moscow, 1970.
Nukleazy mikroorganizmov. Moscow, 1974.


C587H909N171O197S12 An enzyme that catalyzes the depolymerization of ribonucleic acid.
References in periodicals archive ?
The RNase H2 enzyme cleaves only the primer that is exactly matched to the target sequence, unblocking that specific primer for subsequent extension by polymerase.
Since Sennosides A and B were identified as novel dual functions RTIs, we wanted to compare them to known NNRTIs or RNase H inhibitors by using a series of previously described HIV-1 RT mutants.
In the second step, we decided to decrease autolysis during dissection and RNA extraction by using RNA-later as a pancreas RNase inhibitor.
The ultrafilter membrane incorporated in this filter retains colloids, microorganisms, endotoxins, RNA and DNA and removes RNases, which is essential in order to perform ISH.
Plackett-Burman Design (PBD) for screening important medium factors for RNase production
The results of this investigation demonstrate the use of a multiplex qPCR assay, the Multiplex TREC qPCR, with an internal QC, the RNase P gene RPPH1, for use in population-based NBS for detection of SCID.
Inhibition of RNase H activity and viral replication by single mutations in the 3' region of Moloney murine leukemia virus reverse transcriptase.
The denaturation profiles of 10 [micro]g RNAse A, BSA, and total oyster heart protein are shown in Figure 5.
RNase L in health and disease: what did we learn recently?
We are also indebted to our shareholders who supported us over the years, especially in acquiring the patent in 2006 that describes the compounds that inhibit HIV RNase H.
001 [micro]g of RNase A (Qiagen, Hilden, Germany) and 1 [micro]L (2 U) of Turbo DNA-free DNase I (Ambion, Austin, TX, USA) with 1x Turbo DNA-free buffer were incubated at 37[degrees]C for 30 min under conditions that prevented destruction of viral RNA in the viral particles.