• The Korean Journal of Pharmacology
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• v.8 no.1
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• pp.59-62
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• 1972

This study was undertaken to observe the effect of xanthine such as caffeine and aminophylline on the activity of carbonic anhydrase in the kidney and stomach of the mouse. Carbonic anhydrase activities were measured by Philpot & Philpot method (1936). The results of this experiment were as follows: 1. The activity of carbonic anhydrase in the kidney of the mouse was silightly inhibited by the administration of caffeine (0.1 mg/gm, B.W.) or aminophylline (0.08 mg/gm, B.W.). The inhibition was more pronounced by the administration of aminophylline than that of caffeine. 2. In the stomach, there was no significant change in the activity of the carbonic anhydrase after the administration of either caffeine or aminophylline.

• Journal of Integrative Natural Science
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• v.9 no.4
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• pp.268-274
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• 2016

Filariasis causing nematode Brugia malayi is shown to harbor wolbachia bacteria as symbionts. The sequenced genome of the wolbachia endosymbiont from B.malayi (wBm) offers an unprecedented opportunity to identify new wolbachia drug targets. Hence the enzyme carbonic anhydrase from wolbachia endosymbiont of Brugia malayi (wBm) which is responsible for the reversible interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa) is chosen as the drug target for filariasis. This enzyme is thought to play critical functions in bacteria by involving in various steps of their life cycle which are important for survival, The 3D structure of wBm carbonic anhydrase is predicted by selecting a suitable template using the similarity search tool, BLAST. The BLAST results shows a hexapeptide transferase family protein from Anaplasma phagocytophilum (PDB ID: 3IXC) having 77% similarity and 54% identity with wBm carbonic anhydrase. Hence the above enzyme is chosen as the template and the 3D structure of carbonic anhydrase is predicted by the tool Modeller9v7. Since the three dimensional structure of carbonic anhydrase from wolbachia endosymbiont of Brugia malayi has not yet solved, attempts were made to predict this protein. The predicted structure is validated and also molecular docking studies are carried out with the suitable inhibitors that have been solved experimentally.

• Food Science and Biotechnology
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• v.14 no.4
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• pp.551-553
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• 2005

Carbonic anhydrase III was found in liver of flounder, Limanda yokohamae. Protein was isolated from cytosolic extracts and identified using SDS-PAGE and isolectric focusing. Specific protein bands with molecular weight of 30 kDa and pIs of 7.0 and 6.5 were detected by Western blotting. This is the first report of identification of carbonic anhydrase III from L. yokohamae.

• The Korean Journal of Physiology
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• v.14 no.2
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• pp.1-5
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• 1980

This study was undertaken to investigate the influence of prostaglandin $E_1(PGE_1)$ upon the activity of carbonic anhydrase and upon the inhibitory action of acetazolamide on carbonic anhydrase. The heparinized blood was sampled by cardiac puncture from Sprague-Dawley strain rats under ether anesthesia and was hemolysed by adding distilled water 1,000 times the amount of the blood. The activity of carbonic anhydrase of 0.1 ml of the hemolysate was measured by Maren's simplified micro-method. In the first experiment, the 7 rats were used, and the activity was measured by adding 0.1 ml of various concentrations of $PGE_1$(0.5, 1.25, 2.5, 5.0, 10 and $20\;{\mu}g/ml$). In the second experiment, the 6 rats were used and the activity was measured by adding 0.1 ml of $PGE_1(5\;{\mu}g/ml)$ and 0.1 ml of acetazolamide$(6{\times}10^{-7}M/l)$ respectively or simultaneously. Obtained results were as follows: 1) The activity of carbonic anhydrase was significantly inhibited by $PGE_1$ at doses of $0.5{\sim}10\;{\mu}g/ml$, maximally at a dose of $2.5\;{\mu}g/ml$, but inhibition was no more observed at a dose of $20\;{\mu}g/ml$. 2) The activity of the acetazolamide group was significantly less than that of the control group. 3) The activity of the $PGE_1+acetazolamide$ group was significantly less than those of the $PGE_1$ group and the acetazolamide group. It is inferred from the above results that the $PGE_1$ inhibits the activity of carbonic anhydrase dose-dependently and strengthens the inhibitory effect of acetazolamide on carbonic anhydrase.

• Bulletin of the Korean Chemical Society
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• v.25 no.5
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• pp.711-714
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• 2004

Peroxynitrite enters erythrocytes through band 3 anion exchanger and oxidizes cytosolic proteins therein. As a protein associated with band 3, carbonic anhydrase II may suffer from peroxynitrite-induced oxidative damages. Esterase activity of carbonic anhydrase II decreased as the concentration of peroxynitrite increased. Neither hydrogen peroxide nor hypochlorite affected the enzyme activity. Inactivation of the enzyme was in parallel with the release of zinc ion, which is a component of the enzyme's active site. SDS-PAGE of peroxynitrite-treated samples showed no indication of fragmentation but non-denaturing PAGE exhibited new bands with lower positive charges. Western analysis demonstrated that nitration of tyrosine residues increased with the peroxynitrite concentration but the sites of nitration could not be determined. Instead MALDI-TOF analysis identified tryptophan-245 as a site of nitration. Such modification of tryptophan residues is responsible for the decrease in tryptophan fluorescence. These results demonstrate that peroxynitrite nitrates tyrosine and tryptophan residues of carbonic anhydrase II without causing fragmentation or dimerization. The peroxynitrite-induced inactivation of the enzyme is primarily due to the release of zinc ion in the enzyme's active site.

• The Korean Journal of Food And Nutrition
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• v.29 no.1
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• pp.33-36
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• 2016

Carbonic anhydrase is essential for the cellular transportation of hydrogen and bicarbonate ions and plays a key role in a wide variety of physiological processes. Rainbow trout, Oncorhynchus mykiss is an important freshwater fish in aquaculture industry and is known to be one of the most susceptible species to environmental contamination. In this study, carbonic anhydrase was detected in the kidney and intestine of rainbow trout. Carbonic anhydrase was isolated from cytosolic proteins and identified by using SDS-PAGE, isoelectric focusing, and immunohistochemical methods. A specific protein band with molecular weight of 30 kDa and pI of 7.0 was detected by Western blotting. The immunohistochemical results showed that carbonic anhydrase was located at various cells in the kidney and intestine of rainbow trout.

• Journal of Korean Society of Environmental Engineers
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• v.39 no.11
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• pp.607-612
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• 2017

The effect of carbonic anhydrase on $CO_2$ absorption rates and the heat of reaction were evaluated in various amine solutions for post combustion $CO_2$ capture process. The $CO_2$ absorption rate was analyzed in 30 wt% MEA, AMP, DMEA, MDEA aqueous solutions with and without carbonic anhydrase (250 mg/L) from bovine erythrocyte. $CO_2$ absorption rates were increased in all solutions with carbonic anhydrase. The effect of carbonic anhydrase on absorption rates was more in tertiary amine (DMEA and MDEA) solutions than in primary amine (MEA) and hindered amine (AMP) solutions. The heat of reaction of MEA, DMEA, MDEA aqueous solutions with and without carbonic anhydrase were measured using reaction calorimeter. Carbonic anhydrase decreased the heat of absorption in all solutions. The results suggested that tertiary amines that have the excellent desorption ability were suitable for applying carbonic anhydrase to the post combustion $CO_2$ capture process and the effect of carbonic anhydrase was best in MDEA solution.

• The Korean Journal of Pharmacology
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• v.11 no.2
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• pp.1-8
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• 1975

This study was carried out to observe the effect of testosterone on carbonic anhydrase inhibiting action of acetazolamide. Carbonic anhydrase activities in the kidneys of mice were measured by Philpot and Philpot method(1936) at 30, 90 and 150 minutes after intravenous administration of saline(0.5 ml/10 g) or acetazolamide (0.25 mg/10 g) in mice pretreated with testosterone (0.1 mg/10 g). The changes in volume and pH of urine as well as those in urinary electrolytes, such as $Na^+,\;K^+\;and\;Cl^-$ were measured at 15 minutes interval for 150 minutes in the rabbit pretreated with double administrations of testosterone(10 mg/kg), 1 hour and 18 hours, prior to the administration of acetazolamide (10 mg/kg). The results were as follows: 1. Carbonic anhydrase activities in the kidneys of mice of testosterone-pretreated groups were significantly higher than those of acetazolamide-treated group at 30 minutes. No significant changes of carbonic anhydrase activities were observed in testosterone-pretreated groups compared with saline-treated groups. 2. Combined administrations of acetazolamide and testosterone exhibited higher carbonic anhydrase activity than those group of acetazolamide alone in the kidney of mice through observed period of 150 minutes. 3. There were no significant changes in the excretion rate of urine and urinary electrolytes in the group of rabbits with testosterone administerone alone. Urine volume as well as $Na^+\;and\;Cl^-$ excretion rates in the combined treated group of acetazolamide and testosterone were significantly lower than that of acetazolamide group throughout experimental period except 15 minutes after drug administration at the time transient increase was shown. 4. Generally lower $K^+$ excretion rate was observed in the combined treated group of acetazolamide and testosterone compared with the single acetazolamide-treated group and the testosterone-pretreated group shows lowest excretion rate of potassium.

• Journal of Life Science
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• v.23 no.12
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• pp.1557-1561
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• 2013

Carbonic anhydrase isozymes are a widespread, zinc-containing metalloenzyme family. The enzyme catalyzes the reversible inter-conversion of $CO_2$ and $HCO_3$. This reaction is the main role played by CA enzymes in physiological conditions. This enzyme has been found in virtually all organisms, and at least 16 isozymes have been isolated in mammals. Unlike mammals, there is little information available regarding CA isozymes in the tissues of non-mammalian groups, such as fish. Carbonic anhydrase is very important in the osmotic and acid-base regulation in fish. It is well-known that the gills of fish play the most important role in acid-base relevant ion transfer, the transfer of $H^+$ and/or $HCO_3^-$, for the maintenance of systemic pH. Rainbow trout, Oncorhynchus mykiss, is the most important freshwater fish species in the aquaculture industry of Korea, with annual production increasing each year. In addition, environmental toxicology research has shown that rainbow trout is known to be the species that is most susceptible to environmental toxins. Consequently, carbonic anhydrase was detected in rainbow trout, Oncorhynchus mykiss. The isolated protein showed the specific band with a molecular weight of 30 kDa and pI of 7.0, and it was identified as being carbonic anhydrase. The immunohistochemical result demonstrated that the carbonic anhydrase was located in the epithelial cells of the gills.

• KSBB Journal
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• v.29 no.3
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• pp.155-164
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• 2014

Succinic acid, a representative biomass-derived platform chemical, is a major fermentation product of Actinobacillus succinogenes. It is well known that carbon dioxide is consumed during the succinate fermentation, but the biochemical mechanism behind this phenomenon is not yet understood well. In this study, it was found that the addition of carbonic anhydrase (CA)s into media significantly enhances the succinic acid production by A. succinogenes during the fermentation supplied with carbon dioxide. It is likely that the (bi) carbonate produced by the CA activity from gaseous carbon dioxide is favoured by A. succinogenes for consumption and utilization. Therefore, the $MgCO_3$ requirement could be significantly reduced without compromising the succinate productivity. Furthermore, because of too high price of the commercial carbonic anhydrase, it was undertaken to economically overproduce a cyanobacterial carbonic anhydrase by the use of a recombinant Pichia pastoris. An expression vector system was constructed with the carbonic anhydrase gene PCR-cloned from Cyanobacterium Synechocystis sp., and introduced into P. pastoris for fermentation studies. About 95.9 g/L of succinic acid was produced in the production medium with 30 ppm of carbonic anhydrase, approximately 2 fold higher productivity compared to the parallel process with no supplementation of the enzyme. It is expected that this method can provide a valuable way of overcoming inefficiencies inherent in gas supply during $CO_2$-based bioprocesses like succinic acid fermentation.