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 ?
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.
When the number of viral particles in the sample was high, we omitted the RNase A and DNase I treatments and used the RNeasy Mini Kit (Qiagen) for RNA extraction.
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.
Eosinophil-derived neurotoxin is a member of the RNase A superfamily.
It is likely that all the members of the RNase A superfamily family arose from duplication of a single primordial RNase gene.