Search results for "Carbonic anhydrase II"
showing 6 items of 6 documents
Thermodynamic parameters of the interaction between Co(II) bovine carbonic anhydrase and anionic inhibitors
1992
The pH dependence of the apparent affinity constants of perchlorate for cobalt(II)bovine carbonic anhydrase II has been measured by electronic absorption spectroscopy. The obtained data have been analyzed in terms of the ionization of two acidic groups of CoBCAII, and the affinity of perchlorate for the two water-containing species of the enzyme have been estimated. Furthermore, the affinity constants of nitrate, perchlorate, and azide for CoBCAII in the temperature range 5 degrees C-30 degrees C have been determined by spectrophotometric titrations at pH 7. The affinity constants for these ligands decrease with increasing temperatures. The temperature dependence of binding was used to esti…
Interaction of sulphate and chloride with cobalt(II)-carbonic anhydrase
1990
The interaction between Cobalt(II)-Bovine Carbonic Anhydrase II and the inhibitors sulphate and chloride have been investigated through 1H NMR and electronic absorption spectroscopies. Both inhibitors bind to the metal ion forming a 1:1 adduct and the corresponding affinity constants have been determined. These inhibitors interact weakly with CoBCA II and this interaction only occurs at low pH values. The T1 values of the meta-like protons of the coordinated histidines have been measured. The coordination number of the metal ion in the adducts is discussed on the basis of temperature dependence of the isotropic shifts, T1, and molar absorbance values.
Reduction of mdx mouse muscle degeneration by low-intensity endurance exercise: a proteomic analysis in quadriceps muscle of exercised versus sedenta…
2015
By proteomic analysis we found an up-regulation of four carbonic anhydrase-3 (CA3) isoforms and a down-regulation of superoxide dismutase [Cu-Zn] (SODC) in quadriceps of sedentary X-linked muscular dystrophy (mdx) mice as compared with wild–type (WT) mice and the levels were significantly restored to WT values following low-intensity endurance exercise.
Running-induced muscle injury and myocellular enzyme release in rats
1994
The relationships and time course of exercise-induced muscle damage, estimated by beta-glucuronidase activity and microscopy, to muscle swelling, estimated by muscle water content and microscopy, and to the serum activity of creatine kinase (CK) and the concentration of carbonic anhydrase III were studied in rats 2, 12, 48, and 96 h after 90 min of intermittent running uphill (+13.5 degrees) or downhill (-13.5 degrees) at a speed of 17 m/min. The injury was more pronounced in soleus after uphill running and in the red parts of quadriceps femoris and in the white part of vastus lateralis after downhill running, whereas triceps brachii was not damaged. Increase in muscle water content preced…
1H NMR and UV-vis spectroscopic characterization of sulfonamide complexes of nickek(II)-carbonic anhydrase. Resonance assignments based on NOE effects
1992
The binding of acetazolamide, p-fluorobenzensulfonamide, p-toluenesulfonamide, and sulfanilamide to nickel(II)-substituted carbonic anhydrase II has been studied by 1H NMR and electronic absorption spectroscopies. These inhibitors bind to the metal ion forming 1:1 complexes and their affinity constants were determined. The 1H NMR spectra of the formed complexes show a number of isotropically shifted signals corresponding to the histidine ligands. The complexes with benzene-sulfonamides gave rise to very similar 1H NMR spectra. The NMR data suggest that these aromatic sulfonamides bind to the metal ion altering its coordination sphere. In addition, from the temperature dependence of 1H NMR s…
Comparison of the interaction of cobalt bovine carbonic anhydrase II with acetazolamide and methazolamide and the reaction of apoenzyme with cobalt(I…
2003
The metalloenzyme carbonic anhydrase (CA) is an attractive choice for a research-based bioinorganic laboratory course. In this project the interaction of cobalt bovine carbonic anhydrase II (CoBCAII) with acetazolamide and methazolamide and the reaction of apoenzyme with cobalt(II) complexes of acetazolamide and methazolamide is studied by UV-visible spectroscopy. Prior to this spectroscopic study students are given native BCAII, and they prepare apoBCAII and CoBCAII. A major aim is to provide experience in handling metalloproteins and in the study of metal complexes-protein interactions.