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Bovine pancreatic ribonuclease, also often referred to as ''bovine pancreatic ribonuclease A'' or simply ''RNase A'', is a pancreatic ribonuclease enzyme that cleaves single-stranded RNA. Bovine pancreatic ribonuclease is one of the classic model systems of protein science. Two Nobel Prizes in Chemistry have been awarded in recognition of work on bovine pancreatic ribonuclease: in 1972, the Prize was awarded to Christian Anfinsen for his work on protein folding and to Stanford Moore and William Stein for their work on the relationship between the protein's structure and its chemical mechanism;〔(【引用サイトリンク】 publisher = Nobelprize.org )〕 in 1984, the Prize was awarded to Robert Bruce Merrifield for development of chemical synthesis of proteins.〔(【引用サイトリンク】 publisher = Nobelprize.org )〕 ==History== Bovine pancreatic ribonuclease became a common model system in the study of proteins largely because it was extremely stable and could be purified in large quantities. In the 1940s Armour and Company purified a kilogram of protein - a very large quantity, particularly by the protein purification standards of the time - and offered samples at low cost to interested scientists. The ability to have a single lot of purified enzyme made it a predominant model system for protein studies. It remains commonly referred to as ''ribonuclease A'' or ''RNase A'' as the most prominent member of its protein family, known variously as pancreatic ribonuclease, ribonuclease A, or ribonuclease I. Christian Anfinsen's studies of the oxidative folding process of bovine pancreatic ribonuclease laid the groundwork for understanding the relationship between amino acid sequence and a protein's folded three-dimensional structure and solidified the thermodynamic hypothesis of protein folding, according to which the folded form of a protein represents its free energy minimum.〔 RNase A was the first enzyme for which a correct catalytic mechanism was proposed, even before its structure was known. RNase A was the first protein for showing the effects of non-native isomers of peptide bonds preceding proline residues in protein folding. Bovine pancreatic ribonuclease was also the model protein used to work out many spectroscopic methods for assaying protein structure, including absorbance, circular dichroism, Raman, electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopy. It was the first model protein for the development of chemical methods for the study of proteins, such as chemical modification of exposed side chains, antigenic recognition, and limited proteolysis of disordered segments. Ribonuclease S, which is RNase A that has been treated with the protease subtilisin, was the third protein to have its crystallographic structure solved, in 1967. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Bovine pancreatic ribonuclease」の詳細全文を読む スポンサード リンク
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