Oligomerization of Ribonuclease A

Oligomerization of bovine ribonuclease A: structural and functional features of its multimers.

Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active oligomers during lyophilization from aqueous acetic acid solutions. Each oligomeric species is present in at least two conformational isomers. The structures of two dimers and one of the two trimers have been solved, while plausible models have been proposed for the structures of a second trimer ...

Ribonuclease A.

Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity.

Onconase (ONC) is an amphibian member of the bovine pancreatic ribonuclease (RNase A) superfamily that exhibits innate antitumoral activity. ONC has been granted both orphan-drug and fast-track status by the U.S. Food and Drug Administration for the treatment of malignant mesothelioma, and is poised to become the first chemotherapeutic agent based on a ribonuclease. Investigations into the mech...

Active Site of Ribonuclease A

Ribonuclease A (RNase A; EC 3.1.27.5) was perhaps the most studied enzyme of the 20th century and is the best characterized ribonuclease. The “A” in its name refers not to its substrate specificity, but to the predominant form of the enzyme produced by the bovine pancreas. RNase A is unmodified, whereas RNase B, RNase C, and RNase D are mixtures of glycoforms. Because of its availability in lar...

Thermodynamics of immobilized ribonuclease A

Proteins can be bound to surfaces through chemical coupling reactions between the reactive groups of the protein and matrix. In this report, ribonuclease A immobilized on Silica beads, has been used as a model to study the modification of the properties of the enzyme after immobilization. The biological activity has been monitored by studying the binding of the inhibitor ~ytidine-3~-monophospha...