RNase A Solution

Bovine pancreatic ribonuclease A (EC 3.1.27.5; RNase A; RNase I) has been studied in great detail by enzymologists and was the first enzyme to have its complete amino acid sequence determined. This was achieved by William Stein and Stanford Moore in 1963.
RNase A is a member of a superfamily of pancreatic ribonucleases. The Enzyme binds an RNA substrate and localizes a cytidine or uridine to the enzyme active site. The action of two histidines in the active site removes a proton from the 2′-OH of the pyrimidine, causing the formation of a cyclic 2′,3′-phosphate. Phosphate cyclization releases the portion of the RNA chain that is 3′ to the pyrimidine, resulting in cleavage of the RNA strand. The cyclized phosphate is then hydrolyzed creating a 2′-OH and 3′-phosphate on the 3′-terminal ribose of the cleaved RNA.

Features

• CAS Registry Number: 9001-99-4
• Molecular mass: 13.7 kDa (based on amino acid sequence)
• Extinction coefficient (1%): 7.1 (280 nm)
• Isoelectric point: 9.6
• Optimal activity temperature: 60 °C (activity range of 15-70 °C)
• Optimal pH: 7.6 (activity range of 6-10)

For Research Use Only. Not for use in diagnostic procedures.