ribonuclease (pancreatic)

(redirected from RNase A)

ri·bo·nu·cle·ase (pan·cre·at·ic)

(rī'bō-nū'klē-ās pan'krē-at'ik),
An enzyme isolated from the pancreas of ruminants that transfers the 3'-phosphate of a pyrimidine ribonucleotide residue in a polynucleotide from the 5'-position of the adjoining nucleotide to the 2'-position of the pyrimidine nucleotide itself (a transferase, endonuclease action), thus breaking the chain and forming a pyrimidine 2',3'-cyclic phosphate, then (or independently) hydrolyzing this phosphodiester to leave a pyrimidine nucleoside 3'-phosphate residue (phosphodiesterase action); used in cytochemistry to selectively degrade and remove RNA as a control for staining of RNA. End products are nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending Cp or Up.
Synonym(s): RNase A, RNase I
References in periodicals archive ?
In this procedure, the tissue sections were repeatedly washed at 63 C in a solution containing formamide and the unbound probes were removed by incubation with RNase A. A DIG-specific antibody (Roche) was used to detect the DIG-labeled probe.
RNase [T.sub.1] is an extracellular enzyme found by Sato and Egami in 1957 in Taka-Diastase, a commercial enzyme mixture from Aspergillus oryzae, and was shown to hydrolyze specifically the 3'-phosphodiester bond of guanylic acid in RNA unlike the well-studied bovine pancreatic RNase A which is specific for the 3'-cytidylic and 3'-uridylic acids.
(11) These results were similar to those reported for RNase A, suggesting a similar structure-function relationship between the two enzymes.
Due to its ubiquity, RNase A is most commonly favored in tests which are performed to qualify the use of devices, such as pure water systems.
An RNase A stock solution was prepared at 3 mg/mL in a total volume of 200 mL using RNase A and nuclease-free water.
We used 2 experiments to test the efficacy of our method, one with colloidal particles coated with streptavidin to detect biotinylated protein-ribonuclease A (RNase A) and another applying the technique to a commercially available reagent set for RF.
We used biotinylated RNase A in water as a model ligand.
To eliminate contaminating cellular RNA and DNA from the samples, 0.001 [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.
In the example described here, an RNase A enzyme is converted into a zymogen by adding to the enzyme a bridge of amino acids linking the amino and carboxyl termini of the enzyme.
A complex of RNase A with a transition-state analog, uridine vanadate, was also studied using a combination of neutron and x-ray diffraction techniques (14).
MoBio Laboratories, Solana Beach, Calif., used a combination UV oxidation/UF system from Barnstead/Termolyne, Dubuque, Iowa, to test water samples intentional contaminated with high levels of RNase A , RNase TI, DNase 1, and
Eosinophil-derived neurotoxin is a member of the RNase A superfamily.