Cytidine 2′,3′-cyclic monophosphate (2′,3′-CyclicCMP) (2′,3′-cCMP) is used as a model substrate for kinetic analysis of various ribonucleases, especially ribonuclease A.
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pH-Stat titration allows the continuous determination of ribonuclease A activity toward cytidine 2',3'-cyclic monophosphate at high substrate concentrations.
Journal of chromatography. A, 1144(1), 135-142 (2007-01-20)
In gene therapy and DNA vaccination, RNA removal from DNA preparations is vital and is typically achieved by the addition of ribonuclease into the sample. Removal of ribonuclease from DNA samples requires an additional purification step. An alternative is the
In the ribonuclease superfamily, dimericity is a unique feature of bovine seminal RNase (BS-RNase). In about two-thirds of native BS-RNase molecules, the two subunits interchange their N-terminal tails, thus generating domain-swapped dimers (MxM), which mostly responsible for enzyme biological activities
The Journal of biological chemistry, 273(40), 25565-25572 (1998-09-25)
The kinetics of the hydrolysis of cytidine 2',3'-cyclic phosphate (C>p) to 3'-CMP by ribonuclease A are multiphasic at high substrate concentrations. We have investigated these kinetics by determining 3'-CMP formation both spectrophotometrically and by a highly specific and quantitative chemical
Isothermal titration calorimetry (ITC) and progress curve analysis was used to measure the enzyme kinetic parameters (KM and kcat) of the hydrolysis of cCMP by RNase-A, a reaction that includes end-product competitive inhibition by 3'-CMP. The heat generated from injection
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