ribonuclease (pancreatic)

(redirected from pancreatic RNase)

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
Farlex Partner Medical Dictionary © Farlex 2012
References in periodicals archive ?
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.
To assess the sensitivity to protein amounts, denaturation profiles of bovine pancreatic RNAse A were generated with three different amounts of protein: 10 [micro]g, 1 [micro]g, and 100 ng.
Still, it remains unknown whether such differences in the profiles of RNA fragments generated by RNase1 and binase may contribute to their different biological effects, since noncytotoxic pancreatic RNases demonstrated very low immunogenicity [25], did not bind to the cell surface, and were not internalized into cell [26], whereas cytotoxic binase bound to cell membrane receptors, for example, RAS protein subfamily receptors, and effectively permeated cells [8, 27].