胞苷 2',3'-环一磷酸钠盐
胞苷 2',3'-环一磷酸钠盐结构式
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常用名 | 胞苷 2',3'-环一磷酸钠盐 | 英文名 | Cytidine, cyclic2',3'-(hydrogen phosphate), sodium salt |
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| CAS号 | 15718-51-1 | 分子量 | 327.16300 | |
| 密度 | 2.28 g/cm3 | 沸点 | 568.5ºC at 760 mmHg | |
| 分子式 | C9H11N3NaO7P | 熔点 | 245°C (lit.) | |
| MSDS | 美版 | 闪点 | 297.6ºC |
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Increased proteolytic resistance of ribonuclease A by protein engineering.
Protein Eng. 14 , 791-796, (2001) 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 mu... |
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Preparation and characterisation of ribonuclease monolithic bioreactor.
J. Chromatogr. A. 1144 , 135-142, (2007) 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... |
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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.
Anal. Biochem. 305 , 281-284, (2002)
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The subsites structure of bovine pancreatic ribonuclease A accounts for the abnormal kinetic behavior with cytidine 2',3'-cyclic phosphate.
J. Biol. Chem. 273(40) , 25565-72, (1998) 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 high... |
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Influence of the structure of water on the hydrolysis of cytidine 2',3'-phosphate catalysed by bovine pancreatic ribonuclease A.
Eur. J. Biochem. 124(1) , 151-6, (1982) The study of the temperature dependence of the hydrolysis of cytidine 2',3'-phosphate by bovine pancreatic ribonuclease A (EC 3.1.27.5) at pH 7.0 by using the pH-stat method showed a transition at 4 degrees C [J. A. Biosca and C. M. Cuchillo (1980) Biochem. J... |
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Isothermal titration calorimetric study of RNase-A kinetics (cCMP --> 3'-CMP) involving end-product inhibition.
Pharm. Res. 21(9) , 1642-7, (2004) 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 f... |
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BS-RNase tetramers: an example of domain-swapped oligomers.
FEBS Lett. 398(2-3) , 326-32, (1996) 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 mostl... |
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Production of human pancreatic ribonuclease in Saccharomyces cerevisiae and Escherichia coli.
Protein Expr. Purif. 7(3) , 253-61, (1996) 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, synthesiz... |
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Isothermal titration calorimetric study of RNase-A kinetics (cCMP→ 3′-CMP) involving end-product inhibition. Spencer SD, Raffa RB.
Pharmaceut. Res. 21 , 1642-1647, (2004)
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