Bovine carbonic anhydrase

Redpath, J.L. et al. (1975). Role of metal ions in the radiosensitivity of mctalloproteins. Model experiments with bovine carbonic anhydrase. Int. J. Radiat. Biol. 26, 243. 

Fig. 38. Far-UV CD spectra of bovine carbonic anhydrase B in various states. Native,...

Fig. 39. Near-UV CD spectrum of bovine carbonic anhydrase B. Native state, pH 7 (—) acid-denatured state, pH 2 (---). See note in legend to Fig. 38. From Wong and Hamlin (1974). Biochemistry 13, 2678-2683, with permission. 1974, American Chemical Society.

Gudiksen, K.L., Gitlin, I., Moustakas, D.T., Whitesides, G.M. (2006a). Increasing the net charge and decreasing the hydrophobicity of bovine carbonic anhydrase decreases the rate of denaturation with sodium dodecyl sulfate. Biophys. J. 91, 298-310. 

We found that solutions of hen egg white lysozyme, bovine ribonuclease A (RNase A), or a 1 2 mol ratio of bovine carbonic anhydrase lysozyme formed opaque gels within 2 min when mixed with an equal volume of 20% NBF.25,26 Multi-protein tissue surrogates comprised of 50% w/v lysozyme and up to four additional proteins have also been formed (Fowler et al., unpublished results). After overnight fixation, the surrogates were firm and sliced easily with a razor blade for sampling. To determine the optimal... 

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). 

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... 

LZ Avila, Y-H Chu, EC Blossey, GM Whitesides. Use of affinity capillary electrophoresis to determine kinetic and equilibrium constants for binding of arylsulfonamides to bovine carbonic anhydrase. J Med Chem 36 126-133,... 

Fig. 7 Mobility-shift assay for the determination of dissociation constant of the complex between anti-DNP rat monoclonal IgG21) antibody and charged ligands that contained the A-dinitrophenyl group. Mesityl oxide (MO) served as EOF marker, bovine carbonic anhydrase (CAB) and bovine a-lactalbumin (LA) as internal references. The DNP ligands with a charge of —1 (A) und —9 (B), respectively, were used as additives to the running buffer. (Reprinted with permission from Ref. 30. Copyright 1995 American Chemical Society.)...

Bovine carbonic anhydrase is a protein with 18 lysine residues. The 19 peaks in Figure 26-22 arise from unmodified protein (P" ) plus protein with every possible degree of acetylation p(, + , p( +2>, p( +3)- p< +i8)- The voltage applied to the 0.840-m-long capil-... 

Figure 26-22 Protein charge ladder. Bovine carbonic anhydrase was acetylated to give species with charges of n (unacetylated),...

Figure B3.1.3 An isoelectric focusing (IEF) gel, pH 3 to 10. Lane 1, 4 pg purified egg white cystatin. Lane M, broad-range pi standards trypsinogen (pi 9.3), lentil lectin-basic band (pi 8.65), lentil lectin-middle band (pi 8.45), lentil lectin-acidic band (pi 8.15), myoglobin-basic band (pi 7.35 visible as a broad band), myoglobin-acidic band (pi 6.85), human carbonic anhydrase B (pi 6.55), bovine carbonic anhydrase (pi 5.85), a-lactoglobulin A (pi 5.20), soybean trypsin inhibitor (pi 4.55), and amyloglucosidase (pi 3.50) in order shown from top of gel. The pi values of the two purified egg white cystatin isomers were determined to be 6.6 (upper band) and 5.8 (lower band). Adapted from Akpinar (1998) with permission from author.

Carbonic anhydrase is a zinc(II) metalloenzyme which catalyzes the hydration and dehydration of carbon dioxide, C02+H20 H+ + HC03. 25 As a result there has been considerable interest in the metal ion-promoted hydration of carbonyl substrates as potential model systems for the enzyme. For example, Pocker and Meany519 studied the reversible hydration of 2- and 4-pyridinecarbaldehyde by carbonic anhydrase, zinc(II), cobalt(II), H20 and OH. The catalytic efficiency of bovine carbonic anhydrase is ca. 108 times greater than that of water for hydration of both 2- and 4-pyridinecarbaldehydes. Zinc(II) and cobalt(II) are ca. 107 times more effective than water for the hydration of 2-pyridinecarbaldehyde, but are much less effective with 4-pyridinecarbaldehyde. Presumably in the case of 2-pyridinecarbaldehyde complexes of type (166) are formed in solution. Polarization of the carbonyl group by the metal ion assists nucleophilic attack by water or hydroxide ion. Further studies of this reaction have been made,520,521 but the mechanistic details of the catalysis are unclear. Metal-bound nucleophiles (M—OH or M—OH2) could, for example, be involved in the catalysis. 

Table 2. Some properties of human and bovine carbonic anhydrases (34, 64, 66, 85)...

Table 3. Metal ion specificity of bovine carbonic anhydrase B...

Table 4. Stabilities of bovine carbonic anhydrase — anion complexes...

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

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] ... 

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-... 

The active site of bovine carbonic anhydrase consists of a tetrahedrally coordinated zinc ion (1) [27] with a coordinated water molecule whose p(7.5) [28, 29] is con-... 

Figure 7 Effect of salt concentration on migration velocity of DMSO, bovine carbonic anhydrase (BCA), a-lactalbumin (a-LAC), soybean trypsin inhibitor (STI), and ovalbumin (OVA). Conditions column 50 pm i.d. x 340/260 mm, packed with strong anion exchanger mobile phase, 50, 100, and 200 mM NaCI in 5 mM phosphate buffer, pH 7.0 applied voltage, -1 5 kV injection, 6 s at-8 kV UV detection, 200 nm. (Reprinted with permission from Ref. 48, copyright 2000, American Chemical Society.)...

Fig. i Constitutional dynamic chemistry applied to bovine carbonic anhydrase bCA II isozyme and elaboration of constitutional dynamic library (CDL). Precursor amines a-d and aldehydes 1-3 and resulting components of the combinatorial library Ia-c-3a-c. HPLC traces of the final reaction mixtures showing amplification of 3c and 3d (adapted from [49])... 

Fig. 2. Correlation between and molecular mass for globular proteins. In order of increasing mass the proteins are cjrtochrome c. ribonuclease A, myoglobin, bovine carbonic anhydrase, p-lactoglobulin, ovalbumin, hemoglobin, bovine serum albumin and transferrin.

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