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Bovine carbonic anhydrase II

J.D. Badjic and N.M. Kostic, Effects of encapsulation in sol-gel silica glass on esterase activity, conformational stability, and unfolding of bovine carbonic anhydrase II. Chem. Mater. 11, 3671-3679 (1999). [Pg.549]

Fig. 14. Paramagnetic enhancements to water NMRD profiles for solutions of cobalt(II) human carbonic anhydrase I at pH 9.9 and 298 K ( ) (48,49) and for solutions of the nitrate adduct of cobalt(II) bovine carbonic anhydrase II at pH 6.0 and 298 K ( ) (126). The dashed line shows the best fit profile of the former data calculated with including the effect of ZFS, whereas the dotted line shows the best fit profile calculated without including the effect of ZFS. Fig. 14. Paramagnetic enhancements to water NMRD profiles for solutions of cobalt(II) human carbonic anhydrase I at pH 9.9 and 298 K ( ) (48,49) and for solutions of the nitrate adduct of cobalt(II) bovine carbonic anhydrase II at pH 6.0 and 298 K ( ) (126). The dashed line shows the best fit profile of the former data calculated with including the effect of ZFS, whereas the dotted line shows the best fit profile calculated without including the effect of ZFS.
Water NMRD profiles acquired for other complexes and proteins always exhibit the same features of hexaaqua nickel(II). As an example, we report here the profile of the hexa-coordinate nickel(II)-substituted bovine carbonic anhydrase II 54,55) (Fig. 15). As in the aqua complex, (i) the low-field profile is flat, (ii) no dispersion appears, the cOg dispersion being quenched in S = 1 complexes with large static ZFS 56) (see Section I.A.5) and the... [Pg.131]

Abbreviations BCA II bovine carbonic anhydrase II SOD superoxide dismutase TRN transferrin AP alkaline phosphatase Pj inorganic phosphate PDO phthalate dioxygenase E = empty . [Pg.177]

Water H R values have been measured for nickel(II)-substituted bovine carbonic anhydrase II [132,135] (Fig. 5.48), for which the following coordination polyhedron has been proposed [136,137] ... [Pg.188]

Separations of various proteins, such as bovine carbonic anhydrase II, insulin, and lysozyme, have been achieved on a PDMS chip. The PDMS surface was oxidized to become hydrophilic. Since lysozyme is positively charged, the oxi-... [Pg.350]

In a second screening example, Tseng and co-workers [80] demonstrated the use of a PDMS microfluidic reactorto screen bovine carbonic anhydrase II (bCAII) (138) for activity towards the dick reaction of the acetylene 139 and 10 azides (Scheme 6.34). The micro reactor consisted of several components, including a nanoliter rotary mixer, a chaotic mixer, and a microfluidic multiplexer, which enabled discrete aliquots of reactants to be introduced into the micro reaction channel, allowing multiple reactions to be performed in parallel. [Pg.195]

Classification of inhibitors of bovine carbonic anhydrase II according to the electronic spectral properties of the adducts with cobalt(ll) derivatives. ... [Pg.59]

Cd NMR spectra of Cd-substituted bovine carbonic anhydrase II in the presence of N-enriched (A) or N-enriched (B) benzenesulfonamide inhibitor. ... [Pg.73]

N.R., Thompson, G.S., Kalverda, A.P., Warriner, S.L., and Homans, S.W (2008) Residual ligand entropy in the binding of p-substituted benzenesulfonamide ligands to bovine carbonic anhydrase II. Journal of the American Chemical Society,... [Pg.221]

Several bioactive proteins retained their activity and conformation in sol-gel matrices. The sol-gel entrapped heme proteins such as cytochrome c and Mb showed good stability against pH and thermal perturbations compared to protein in solution [29, 55]. The sol-gel caged cytochrome c (cyt c) showed high thermal stability due to the exact fitting of the protein inside the cage, which was controlled by the protein size [56]. Sol-gel encapsulated acid phosphatase [57] and bovine carbonic anhydrase II (BCA II)... [Pg.509]

R. Afrin, M. Alam, and A Ikai, Pretransition and progressive softening of bovine carbonic anhydrase II as probed by single molecule atomic force microscopy. Protein Sci, 14,1447 (2005). [Pg.742]

Relative binding affinities can also be determined using the aformentioned method. Chen et al. " have implemented ESI-FTICR-MS for the determination of relative binding affinities of 16 inhibitors derived from para-substituted benzenesulfonamides towards bovine carbonic anhydrase II in a single experiment using the competition method. [Pg.562]


See other pages where Bovine carbonic anhydrase II is mentioned: [Pg.532]    [Pg.132]    [Pg.152]    [Pg.188]    [Pg.152]    [Pg.81]    [Pg.283]    [Pg.239]    [Pg.74]    [Pg.65]    [Pg.239]    [Pg.509]    [Pg.293]    [Pg.628]    [Pg.254]    [Pg.256]    [Pg.738]    [Pg.82]    [Pg.451]   
See also in sourсe #XX -- [ Pg.74 ]

See also in sourсe #XX -- [ Pg.177 , Pg.178 , Pg.178 , Pg.179 ]




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