메뉴 건너뛰기




Volumn 88, Issue 2, 2012, Pages 255-259

Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide

Author keywords

Ammonium sulfate; Carbonic anhydrase; Enzymically catalyzed capture; Organic solvents; Precipitation

Indexed keywords

AIR PURIFICATION; BLOOD; CALCITE; CALCIUM CARBONATE; CARBON CAPTURE; CARBON DIOXIDE; CARBON DIOXIDE PROCESS; CATALYSIS; CHLORINE COMPOUNDS; ETHANOL; EXTRACTION; HYDRATION; MAMMALS; NITROGEN COMPOUNDS; ORGANIC SOLVENTS; PRECIPITATION (CHEMICAL); SULFUR COMPOUNDS;

EID: 84860251805     PISSN: 00456535     EISSN: 18791298     Source Type: Journal    
DOI: 10.1016/j.chemosphere.2012.03.059     Document Type: Article
Times cited : (33)

References (30)
  • 1
    • 77953132322 scopus 로고    scopus 로고
    • A novel and one-pot synthesis of new 1-tosyl pyrrol-2-one derivatives and analysis of carbonic anhydrase inhibitory potencies
    • Alp C., Ekinci D., Gültekin M.S., Sentürk M., Sahin E., Küfrevioglu ö.I. A novel and one-pot synthesis of new 1-tosyl pyrrol-2-one derivatives and analysis of carbonic anhydrase inhibitory potencies. Bioorg. Med. Chem. 2010, 18:4468-4474.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 4468-4474
    • Alp, C.1    Ekinci, D.2    Gültekin, M.S.3    Sentürk, M.4    Sahin, E.5    Küfrevioglu, Ö.I.6
  • 2
    • 0014011587 scopus 로고
    • Purification and properties of human erythrocyte carbonic anhydrases
    • Armstrong J.M.D., Myers D.V., Verpoorte J.A., Edsall J.T. Purification and properties of human erythrocyte carbonic anhydrases. J. Biol. Chem. 1966, 241:5137-5149.
    • (1966) J. Biol. Chem. , vol.241 , pp. 5137-5149
    • Armstrong, J.M.D.1    Myers, D.V.2    Verpoorte, J.A.3    Edsall, J.T.4
  • 3
    • 53249095401 scopus 로고    scopus 로고
    • In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II
    • Bayram E., Senturk M., Kufrevioglu O.I., Supuran C.T. In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II. Bioorg. Med. Chem. 2008, 16:9101-9105.
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 9101-9105
    • Bayram, E.1    Senturk, M.2    Kufrevioglu, O.I.3    Supuran, C.T.4
  • 4
    • 77957018787 scopus 로고    scopus 로고
    • Antioxidant and antimicrobial peptidic hydrolysates from muscle protein sources and by-products
    • Bernardini R.D., Harnedy P., Bolton D., Kerry J., O'Neill E., Mullen A.M., Hayes M. Antioxidant and antimicrobial peptidic hydrolysates from muscle protein sources and by-products. Food Chem. 2011, 124:1296-1307.
    • (2011) Food Chem. , vol.124 , pp. 1296-1307
    • Bernardini, R.D.1    Harnedy, P.2    Bolton, D.3    Kerry, J.4    O'Neill, E.5    Mullen, A.M.6    Hayes, M.7
  • 6
    • 0031148922 scopus 로고    scopus 로고
    • Comparative effects on intraocular pressure between systemic and topical carbonic anhydrase inhibitors: a clinical masked, cross-over study
    • Centofanti M., Manni G.L., Napoli D., Bucci M.G. Comparative effects on intraocular pressure between systemic and topical carbonic anhydrase inhibitors: a clinical masked, cross-over study. Pharmacol. Res. 1997, 35:481-485.
    • (1997) Pharmacol. Res. , vol.35 , pp. 481-485
    • Centofanti, M.1    Manni, G.L.2    Napoli, D.3    Bucci, M.G.4
  • 7
    • 67650155154 scopus 로고    scopus 로고
    • 2 into water; an alternative to monoethanolamine (MEA) solvents
    • 2 into water; an alternative to monoethanolamine (MEA) solvents. Energ. Procedia 2009, 1:885-892.
    • (2009) Energ. Procedia , vol.1 , pp. 885-892
    • Davy, R.1
  • 9
    • 33748691377 scopus 로고    scopus 로고
    • The in vitro effects of some pesticides on carbonic anhydrase activity of Oncorhynchus mykiss and Cyprinus carpio carpio fish
    • Dogan S. The in vitro effects of some pesticides on carbonic anhydrase activity of Oncorhynchus mykiss and Cyprinus carpio carpio fish. J. Hazard. Mater. 2006, 132:171-176.
    • (2006) J. Hazard. Mater. , vol.132 , pp. 171-176
    • Dogan, S.1
  • 12
    • 38649141522 scopus 로고    scopus 로고
    • Effect of processing on functional properties of animal blood plasma
    • Hoyo P.D., Rendueles M., Díaz M. Effect of processing on functional properties of animal blood plasma. Meat Sci. 2008, 78:522-528.
    • (2008) Meat Sci. , vol.78 , pp. 522-528
    • Hoyo, P.D.1    Rendueles, M.2    Díaz, M.3
  • 14
    • 19544369337 scopus 로고    scopus 로고
    • Proteins, isoleucine, lysine and methionine content of bovine, porcine and poultry blood and their fractions
    • Márquez E., Bracho M., Archile A., Rangel L., Benítez B. Proteins, isoleucine, lysine and methionine content of bovine, porcine and poultry blood and their fractions. Food Chem. 2005, 93:503-505.
    • (2005) Food Chem. , vol.93 , pp. 503-505
    • Márquez, E.1    Bracho, M.2    Archile, A.3    Rangel, L.4    Benítez, B.5
  • 15
    • 84908284616 scopus 로고
    • Carbonic anhydrase. Its preparation and properties
    • Meldrum N.U., Roughton F.J.W. Carbonic anhydrase. Its preparation and properties. J. Physiol. 1933, 80:113-142.
    • (1933) J. Physiol. , vol.80 , pp. 113-142
    • Meldrum, N.U.1    Roughton, F.J.W.2
  • 17
    • 15544371642 scopus 로고    scopus 로고
    • Measurement of erythrocyte carbonic anhydrase isozymes (CA-I and CA-II) in racehorses and riding horses
    • Nishita T., Takahasi M., Kasuya T., Matsui K., Ichihara N., Murakami M., Asari M. Measurement of erythrocyte carbonic anhydrase isozymes (CA-I and CA-II) in racehorses and riding horses. J. Vet. Med. Sci. 2005, 67:63-67.
    • (2005) J. Vet. Med. Sci. , vol.67 , pp. 63-67
    • Nishita, T.1    Takahasi, M.2    Kasuya, T.3    Matsui, K.4    Ichihara, N.5    Murakami, M.6    Asari, M.7
  • 19
    • 3543097391 scopus 로고    scopus 로고
    • A new method for purification of carbonic anhydrase isozymes by affinity chromatography
    • Ozensoy O., Arslan O., Sinan S.O. A new method for purification of carbonic anhydrase isozymes by affinity chromatography. Biochem. (Moscow) 2004, 69:216-219.
    • (2004) Biochem. (Moscow) , vol.69 , pp. 216-219
    • Ozensoy, O.1    Arslan, O.2    Sinan, S.O.3
  • 20
    • 0025318111 scopus 로고
    • Purification of soluble enzymes from erythrocyte hemolysates by three phase partitioning
    • Pol M.C., Deutsch H.F., Visser L. Purification of soluble enzymes from erythrocyte hemolysates by three phase partitioning. Int. J. Biochem. 1990, 22:179-185.
    • (1990) Int. J. Biochem. , vol.22 , pp. 179-185
    • Pol, M.C.1    Deutsch, H.F.2    Visser, L.3
  • 22
    • 0346761424 scopus 로고
    • The manometric determination of the activity of carbonic anhydrase under varied conditions
    • Roughton F.J.W., Booth V.H. The manometric determination of the activity of carbonic anhydrase under varied conditions. Biochem. J. 1946, 40:309-319.
    • (1946) Biochem. J. , vol.40 , pp. 309-319
    • Roughton, F.J.W.1    Booth, V.H.2
  • 23
    • 34248166603 scopus 로고    scopus 로고
    • In vitro inhibition of the carbonic anhydrase from saanen goat (Capra hircus) with pesticides
    • Sinan S., Gencer N., Turan Y., Arslan O. In vitro inhibition of the carbonic anhydrase from saanen goat (Capra hircus) with pesticides. Pest. Biochem. Physiol. 2007, 88:307-311.
    • (2007) Pest. Biochem. Physiol. , vol.88 , pp. 307-311
    • Sinan, S.1    Gencer, N.2    Turan, Y.3    Arslan, O.4
  • 24
    • 0033823229 scopus 로고    scopus 로고
    • Prokaryotic carbonic anhydrases
    • Smith K.S. Prokaryotic carbonic anhydrases. FEMS Microbiol. Rev. 2000, 24:335-366.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 335-366
    • Smith, K.S.1
  • 25
    • 12144271355 scopus 로고    scopus 로고
    • Temporal dependence in uncoupling of blood volume and oxygenation during interictal epileptiform events in rat neocortex
    • Suh M., Bahar S., Mehta A.D., Schwartz T.H. Temporal dependence in uncoupling of blood volume and oxygenation during interictal epileptiform events in rat neocortex. J. Neurosci. 2005, 25:68-77.
    • (2005) J. Neurosci. , vol.25 , pp. 68-77
    • Suh, M.1    Bahar, S.2    Mehta, A.D.3    Schwartz, T.H.4
  • 26
    • 0015235687 scopus 로고
    • Purification and properties of carbonic anhydrase from sheep erythrocytes
    • Tanis R.J., Tashian R.E. Purification and properties of carbonic anhydrase from sheep erythrocytes. Biochemistry 1971, 10:4852-4858.
    • (1971) Biochemistry , vol.10 , pp. 4852-4858
    • Tanis, R.J.1    Tashian, R.E.2
  • 27
    • 84909509949 scopus 로고
    • Comparative aspects of the primary structures and activities of mammalian carbonic anhydrases
    • Tashian R.E., Tanis R.J., Ferrell R.E. Comparative aspects of the primary structures and activities of mammalian carbonic anhydrases. Alfred. Benson. Symp. 1972, 4:353.
    • (1972) Alfred. Benson. Symp. , vol.4 , pp. 353
    • Tashian, R.E.1    Tanis, R.J.2    Ferrell, R.E.3
  • 29
    • 33646166939 scopus 로고    scopus 로고
    • Conformational changes and inactivation of bovine carbonic anhydrase II in 2,2,2-trifluoroethanol solutions
    • Wei X., Ding S., Jiang Y., Zeng X.G., Zhou H.M. Conformational changes and inactivation of bovine carbonic anhydrase II in 2,2,2-trifluoroethanol solutions. Biochem. (Moscow) 2006, 71:77-82.
    • (2006) Biochem. (Moscow) , vol.71 , pp. 77-82
    • Wei, X.1    Ding, S.2    Jiang, Y.3    Zeng, X.G.4    Zhou, H.M.5
  • 30
    • 84957894255 scopus 로고
    • Electrometric and colorimetric determination of carbonic anhydrase
    • Wilbur K.M., Anderson N.G. Electrometric and colorimetric determination of carbonic anhydrase. J. Biol. Chem. 1948, 176:147-154.
    • (1948) J. Biol. Chem. , vol.176 , pp. 147-154
    • Wilbur, K.M.1    Anderson, N.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.