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.
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
Although highly stable toward unfolding, native ribonuclease A is known to be cleaved by unspecific proteases in the flexible loop region near Ala20. With the aim to create a protease-resistant ribonuclease A, Ala20 was substituted for Pro by site-directed mutagenesis.
Protein expression and purification, 7(3), 253-261 (1996-05-01)
Human pancreatic ribonuclease (HP-RNase) has considerable promise as a therapeutic agent. Structure-function analyses of HP-RNase have been impeded by the difficulty of obtaining the enzyme from its host. Here, a gene encoding HP-RNase was designed, synthesized, and inserted into two
pH-Stat titration allows the continuous determination of ribonuclease A activity toward cytidine 2',3'-cyclic monophosphate at high substrate concentrations.
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
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