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Volumn 31, Issue 5, 2016, Pages 689-694

A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization

Author keywords

Affinity chromatography; carbonic anhydrase; characterization; inhibitor

Indexed keywords

2 DIETHYLAMINOETHANOL; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE I; CARBONATE DEHYDRATASE II; CARBONATE DEHYDRATASE III; CARBONATE DEHYDRATASE IV; CARBONATE DEHYDRATASE IX; CARBONATE DEHYDRATASE V; CARBONATE DEHYDRATASE X; CARBONATE DEHYDRATASE XII; ENZYME INHIBITOR; GLUTATHIONE TRANSFERASE; ISOENZYME; SEPHADEX; SEPHAROSE; SULFANILAMIDE; UNCLASSIFIED DRUG; ISOPROTEIN;

EID: 84976515432     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.3109/14756366.2015.1059333     Document Type: Review
Times cited : (139)

References (95)
  • 2
    • 84865850354 scopus 로고    scopus 로고
    • Structure-based drug discovery of carbonic anhydrase inhibitors
    • C.T.Supuran. Structure-based drug discovery of carbonic anhydrase inhibitors. J Enzyme Inhib Med Chem 2012;27:759–72
    • (2012) J Enzyme Inhib Med Chem , vol.27 , pp. 759-772
    • Supuran, C.T.1
  • 3
    • 38849143765 scopus 로고    scopus 로고
    • Carbonic anhydrases: novel therapeutic applications for inhibitors and activators
    • C.T.Supuran. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 2008;7:168–81
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 168-181
    • Supuran, C.T.1
  • 4
    • 0001293394 scopus 로고
    • Purification and properties of bovine erythrocyte carbonic anhydrase
    • S.Lindskog. Purification and properties of bovine erythrocyte carbonic anhydrase. Biochim Biophys Acta 1960;39:218–26
    • (1960) Biochim Biophys Acta , vol.39 , pp. 218-226
    • Lindskog, S.1
  • 5
    • 0011863785 scopus 로고
    • Purification and properties of carbonic anhydrase from human erythrocytes
    • P.O.Nyman. Purification and properties of carbonic anhydrase from human erythrocytes. Biochim Biophys Acta 1961;52:1–12
    • (1961) Biochim Biophys Acta , vol.52 , pp. 1-12
    • Nyman, P.O.1
  • 7
    • 0011819421 scopus 로고
    • Zinc binding and the sulfhydryl group of human carbonic anhydrase
    • E.E.Rickli, J.T.Edsall. Zinc binding and the sulfhydryl group of human carbonic anhydrase. J Biol Chem 1962;237:258–60
    • (1962) J Biol Chem , vol.237 , pp. 258-260
    • Rickli, E.E.1    Edsall, J.T.2
  • 8
    • 0000046295 scopus 로고
    • Carbonic anhydrases from human erythrocytes. Preparation and properties of two enzymes
    • E.E.Rickli, S.A.Ghazanfar, B.H.Gibbons,. Carbonic anhydrases from human erythrocytes. Preparation and properties of two enzymes. J Biol Chem 1964;239:1065–78
    • (1964) J Biol Chem , vol.239 , pp. 1065-1078
    • Rickli, E.E.1    Ghazanfar, S.A.2    Gibbons, B.H.3
  • 9
    • 0013830847 scopus 로고
    • On carbonic anhydrases of human erythrocytes. I. Isolation and purification
    • G.Laurent, M.Charrel, F.Luccioni,. On carbonic anhydrases of human erythrocytes. I. Isolation and purification. Bull Soc Chim Biol (Paris) 1965;47:1101–24
    • (1965) Bull Soc Chim Biol (Paris) , vol.47 , pp. 1101-1124
    • Laurent, G.1    Charrel, M.2    Luccioni, F.3
  • 10
    • 0002940291 scopus 로고
    • Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution
    • K.K.Kannan, B.Notsrand, K.Fridborg,. Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution. Proc Natl Acad Sci USA 1975;72:51–5
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 51-55
    • Kannan, K.K.1    Notsrand, B.2    Fridborg, K.3
  • 11
    • 0000750472 scopus 로고
    • Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase
    • P.Nyman, S.Lindskog. Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase. Biochim Biophys Acta 1964;85:141–51
    • (1964) Biochim Biophys Acta , vol.85 , pp. 141-151
    • Nyman, P.1    Lindskog, S.2
  • 12
    • 0015496940 scopus 로고
    • Amino acid sequence of human erythrocyte carbonic anhydrase B
    • B.Andersson, P.O.Nyman, L.Strid. Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem Biophys Res Commun 1972;48:670–7
    • (1972) Biochem Biophys Res Commun , vol.48 , pp. 670-677
    • Andersson, B.1    Nyman, P.O.2    Strid, L.3
  • 13
    • 0015491585 scopus 로고
    • Crystal structure of human carbonic anhydrase C
    • A.Liljas, K.K.Kannan, P.C.Bergstén,. Crystal structure of human carbonic anhydrase C. Nat New Biol 1972;235:131–7
    • (1972) Nat New Biol , vol.235 , pp. 131-137
    • Liljas, A.1    Kannan, K.K.2    Bergstén, P.C.3
  • 15
    • 0015935332 scopus 로고
    • Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B
    • K.T.Lin, H.F.Deutsch. Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. J Biol Chem 1973;248:1885–93
    • (1973) J Biol Chem , vol.248 , pp. 1885-1893
    • Lin, K.T.1    Deutsch, H.F.2
  • 16
    • 0016256721 scopus 로고
    • Human carbonic anhydrases. XII. The complete primary structure of the C isozyme
    • K.T.Lin, H.F.Deutsch. Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem 1974;249:2329–37
    • (1974) J Biol Chem , vol.249 , pp. 2329-2337
    • Lin, K.T.1    Deutsch, H.F.2
  • 17
    • 0016202087 scopus 로고
    • Catalytic activity and inhibition of carbonic anhydrase of rat tissues
    • L.C.Garg. Catalytic activity and inhibition of carbonic anhydrase of rat tissues. Biochem Pharmacol 1974;23:3153–61
    • (1974) Biochem Pharmacol , vol.23 , pp. 3153-3161
    • Garg, L.C.1
  • 18
    • 0016062658 scopus 로고
    • The effect of sex hormones on rat liver carbonic anhydrase
    • L.C.Garg. The effect of sex hormones on rat liver carbonic anhydrase. J Pharmacol Exp Ther 1974;189:557–62
    • (1974) J Pharmacol Exp Ther , vol.189 , pp. 557-562
    • Garg, L.C.1
  • 19
    • 0016991487 scopus 로고
    • Mammalian carbonic anhydrase isozymes: evidence for a third locus
    • R.S.Holmes. Mammalian carbonic anhydrase isozymes: evidence for a third locus. J Exp Zool 1976;197:289–95
    • (1976) J Exp Zool , vol.197 , pp. 289-295
    • Holmes, R.S.1
  • 20
    • 0015522574 scopus 로고
    • Pseudoisoenzymes of rabbit muscle phosphoglucose isomerase
    • M.N.Balckburn, J.M.Chirgwin, G.T.James,. Pseudoisoenzymes of rabbit muscle phosphoglucose isomerase. J Biol Chem 1972;247:1170–9
    • (1972) J Biol Chem , vol.247 , pp. 1170-1179
    • Balckburn, M.N.1    Chirgwin, J.M.2    James, G.T.3
  • 21
    • 0017371103 scopus 로고
    • Basic muscle protein, a third genetic locus isoenzyme of carbonic anhydrase?
    • M.K.Koester, A.M.Register, E.A.Noltmann. Basic muscle protein, a third genetic locus isoenzyme of carbonic anhydrase? Biochem Biophys Res Commun 1977;76:196–204
    • (1977) Biochem Biophys Res Commun , vol.76 , pp. 196-204
    • Koester, M.K.1    Register, A.M.2    Noltmann, E.A.3
  • 22
    • 0018686821 scopus 로고
    • A novel carbonic anhydrase from the ovine parotid gland
    • R.T.Fernley, R.D.Wright, J.P.Coghlan. A novel carbonic anhydrase from the ovine parotid gland. FEBS Lett 1979;105:299–302
    • (1979) FEBS Lett , vol.105 , pp. 299-302
    • Fernley, R.T.1    Wright, R.D.2    Coghlan, J.P.3
  • 23
    • 0023132339 scopus 로고
    • Purification and characterization of human salivary carbonic anhydrase
    • H.Murakami, W.S.Sly. Purification and characterization of human salivary carbonic anhydrase. J Biol Chem 1987;262:1382–8
    • (1987) J Biol Chem , vol.262 , pp. 1382-1388
    • Murakami, H.1    Sly, W.S.2
  • 24
    • 0020456358 scopus 로고
    • Membrane-associated carbonic anhydrase purified from bovine lung
    • P.L.Whitney, T.V.Briggle. Membrane-associated carbonic anhydrase purified from bovine lung. J Biol Chem 1982;257:12056–9
    • (1982) J Biol Chem , vol.257 , pp. 12056-12059
    • Whitney, P.L.1    Briggle, T.V.2
  • 25
    • 0024539683 scopus 로고
    • Renal membrane-bound carbonic anhydrase. Purification and properties
    • P.J.Wistrand, K.G.Knuuttila. Renal membrane-bound carbonic anhydrase. Purification and properties. Kidney Int 1989;35:851–9
    • (1989) Kidney Int , vol.35 , pp. 851-859
    • Wistrand, P.J.1    Knuuttila, K.G.2
  • 26
    • 0025330670 scopus 로고
    • Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney
    • X.L.Zhu, W.S.Sly. Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney. J Biol Chem 1990;265:8795–801
    • (1990) J Biol Chem , vol.265 , pp. 8795-8801
    • Zhu, X.L.1    Sly, W.S.2
  • 27
    • 0026342073 scopus 로고
    • Characterization of human gene for a newly discovered carbonic anhydrase, CA VII, and its location to chromosome 16
    • J.C.Montgomery, P.J.Venta, R.L.Eddy,. Characterization of human gene for a newly discovered carbonic anhydrase, CA VII, and its location to chromosome 16. Genomics 1991;11:835–48
    • (1991) Genomics , vol.11 , pp. 835-848
    • Montgomery, J.C.1    Venta, P.J.2    Eddy, R.L.3
  • 28
    • 0026561063 scopus 로고
    • A novel quasi-viral agent, MaTu, is a two-component system
    • S.Pastoreková, Z.Závadová, M.Kostál,. A novel quasi-viral agent, MaTu, is a two-component system. Virology 1992;187:620–6
    • (1992) Virology , vol.187 , pp. 620-626
    • Pastoreková, S.1    Závadová, Z.2    Kostál, M.3
  • 29
    • 0029975564 scopus 로고    scopus 로고
    • Human MN/CA9 gene, a novel member of the carbonic anhydrase family: structure and exon to protein domain relationships
    • R.Opavský, S.Pastoreková, V.Zelník,. Human MN/CA9 gene, a novel member of the carbonic anhydrase family: structure and exon to protein domain relationships. Genomics 1996;33:480–7
    • (1996) Genomics , vol.33 , pp. 480-487
    • Opavský, R.1    Pastoreková, S.2    Zelník, V.3
  • 30
    • 0041062296 scopus 로고    scopus 로고
    • Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers
    • O.Tureci, U.Sahin, E.Vollmar,. Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers. Proc Natl Acad Sci USA 1998;95:7608–13
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7608-7613
    • Tureci, O.1    Sahin, U.2    Vollmar, E.3
  • 31
    • 0032884201 scopus 로고    scopus 로고
    • Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1
    • K.Fujikawa-Adachi, I.Nishimori, T.Taguchi,. Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1. Genomics 1999;61:74–81
    • (1999) Genomics , vol.61 , pp. 74-81
    • Fujikawa-Adachi, K.1    Nishimori, I.2    Taguchi, T.3
  • 32
    • 0033025733 scopus 로고    scopus 로고
    • Isolation and characterization of CAXIV, a novel membrane-bound carbonic anhydrase from mouse kidney
    • K.Mori, Y.Ogawa, K.Ebihara,. Isolation and characterization of CAXIV, a novel membrane-bound carbonic anhydrase from mouse kidney. J Biol Chem 1999;274:15701–5
    • (1999) J Biol Chem , vol.274 , pp. 15701-15705
    • Mori, K.1    Ogawa, Y.2    Ebihara, K.3
  • 33
    • 0027183940 scopus 로고
    • Human mitochondrial carbonic anhydrase: cDNA cloning, expression, subcellular localization, and mapping to chromosome 16
    • Y.Nagao, J.S.Platero, A.Waheed,. Human mitochondrial carbonic anhydrase: cDNA cloning, expression, subcellular localization, and mapping to chromosome 16. Proc Natl Acad Sci USA 1993;90:7623–7
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7623-7627
    • Nagao, Y.1    Platero, J.S.2    Waheed, A.3
  • 34
    • 0028019020 scopus 로고
    • Catalytic properties of mouse carbonic anhydrase V
    • R.W.Heck, S.M.Tanhauser, R.Manda,. Catalytic properties of mouse carbonic anhydrase V. J Biol Chem 1994;269:24742–6
    • (1994) J Biol Chem , vol.269 , pp. 24742-24746
    • Heck, R.W.1    Tanhauser, S.M.2    Manda, R.3
  • 35
    • 0033597814 scopus 로고    scopus 로고
    • Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome X
    • K.Fujikawa-Adachi, I.Nishimori, T.Taguchi,. Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome X. J Biol Chem 1999;274:21228–33
    • (1999) J Biol Chem , vol.274 , pp. 21228-21233
    • Fujikawa-Adachi, K.1    Nishimori, I.2    Taguchi, T.3
  • 36
    • 9144220136 scopus 로고    scopus 로고
    • Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family
    • J.Lehtonen, B.Shen, M.Vihinen,. Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family. J Biol Chem 2004;279:2719–27
    • (2004) J Biol Chem , vol.279 , pp. 2719-2727
    • Lehtonen, J.1    Shen, B.2    Vihinen, M.3
  • 37
    • 84910949318 scopus 로고
    • Die Bindungsweise des Kohlendioxyds im Blute
    • O.M.Henriques. Die Bindungsweise des Kohlendioxyds im Blute. Berlin: Biochem Ztschrft 1928;200:1–24
    • (1928) Berlin: Biochem Ztschrft , vol.200 , pp. 1-24
    • Henriques, O.M.1
  • 38
    • 0042250480 scopus 로고
    • Studies of gas and electrolyte equilibria in blood. XVI. The evolution of carbon dioxide from blood and buffer solutions
    • D.D.Van Slyke, J.A.Hawkins. Studies of gas and electrolyte equilibria in blood. XVI. The evolution of carbon dioxide from blood and buffer solutions. J Biol Chem 1930;87:265–79
    • (1930) J Biol Chem , vol.87 , pp. 265-279
    • Van Slyke, D.D.1    Hawkins, J.A.2
  • 40
    • 84908284616 scopus 로고
    • Carbonic anhydrase. Its preparation and properties
    • N.U.Meldrum, F.J.Roughton. Carbonic anhydrase. Its preparation and properties. J Physiol 1933;80:113–42
    • (1933) J Physiol , vol.80 , pp. 113-142
    • Meldrum, N.U.1    Roughton, F.J.2
  • 41
    • 51149187338 scopus 로고
    • Carbonic anhydrase
    • D.Keilin, T.Mann. Carbonic anhydrase. Nature 1939;144:442–3
    • (1939) Nature , vol.144 , pp. 442-443
    • Keilin, D.1    Mann, T.2
  • 42
    • 0001119497 scopus 로고
    • Carbonic anhydrase. Purification and nature of the enzyme
    • D.Keilin, T.Mann. Carbonic anhydrase. Purification and nature of the enzyme. Biochem J 1940;34:1163–76
    • (1940) Biochem J , vol.34 , pp. 1163-1176
    • Keilin, D.1    Mann, T.2
  • 43
    • 0014430015 scopus 로고
    • Purification and properties of horse erythrocyte carbonic anhydrases
    • A.J.Furth. Purification and properties of horse erythrocyte carbonic anhydrases. J Biol Chem 1968;243:4832–41
    • (1968) J Biol Chem , vol.243 , pp. 4832-4841
    • Furth, A.J.1
  • 44
    • 0000601071 scopus 로고
    • Affinity chromatography of carbonic anhydrase
    • S.O.Falkbring, P.O.Göthe, P.O.Nyman,. Affinity chromatography of carbonic anhydrase. FEBS Lett 1972;24:229–35
    • (1972) FEBS Lett , vol.24 , pp. 229-235
    • Falkbring, S.O.1    Göthe, P.O.2    Nyman, P.O.3
  • 45
    • 0015955686 scopus 로고
    • Affinity chromatography of carbonic anhydrase
    • P.L.Whitney. Affinity chromatography of carbonic anhydrase. Anal Biochem 1974;57:467–76
    • (1974) Anal Biochem , vol.57 , pp. 467-476
    • Whitney, P.L.1
  • 46
    • 0014670360 scopus 로고
    • Human carbonic anhydrases. II. Some physicochemical properties of native isozymes and of similar isozymes generated in vitro
    • S.Funakoshi, H.F.Deutsch. Human carbonic anhydrases. II. Some physicochemical properties of native isozymes and of similar isozymes generated in vitro. J Biol Chem 1969;244:3438–46
    • (1969) J Biol Chem , vol.244 , pp. 3438-3446
    • Funakoshi, S.1    Deutsch, H.F.2
  • 47
    • 0014888527 scopus 로고
    • The purification and properties of carbonic anhydrases from guinea-pig erythrocytes and mucosae of the gastrointestinal tract
    • M.J.Carter, D.S.Parsons. The purification and properties of carbonic anhydrases from guinea-pig erythrocytes and mucosae of the gastrointestinal tract. Biochem J 1970;120:797–808
    • (1970) Biochem J , vol.120 , pp. 797-808
    • Carter, M.J.1    Parsons, D.S.2
  • 48
    • 0015239830 scopus 로고
    • Elasmobranch carbonic anhydrase. Purification and properties of the enzyme from two species of shark
    • J.R.Maynard, J.E.Coleman. Elasmobranch carbonic anhydrase. Purification and properties of the enzyme from two species of shark. J Biol Chem 1971;246:4455–64
    • (1971) J Biol Chem , vol.246 , pp. 4455-4464
    • Maynard, J.R.1    Coleman, J.E.2
  • 49
    • 0017378545 scopus 로고
    • Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B
    • R.G.Khalifah, D.J.Strader, S.H.Bryant,. Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B. Biochemistry 1977;16:2241–7
    • (1977) Biochemistry , vol.16 , pp. 2241-2247
    • Khalifah, R.G.1    Strader, D.J.2    Bryant, S.H.3
  • 50
    • 0016642468 scopus 로고
    • An improved method for the purification of carbonic anhydrase isozymes by affinity chromatography
    • W.R.Osborne, R.E.Tashian. An improved method for the purification of carbonic anhydrase isozymes by affinity chromatography. Anal Biochem 1975;64:297–303
    • (1975) Anal Biochem , vol.64 , pp. 297-303
    • Osborne, W.R.1    Tashian, R.E.2
  • 51
    • 0018358044 scopus 로고
    • Kinetic and magnetic properties of cobalt(III) ion in the active site of carbonic anhydrase
    • H.Shinar, G.Navon. Kinetic and magnetic properties of cobalt(III) ion in the active site of carbonic anhydrase. Eur J Biochem 1979;93:313–22
    • (1979) Eur J Biochem , vol.93 , pp. 313-322
    • Shinar, H.1    Navon, G.2
  • 52
    • 0020655228 scopus 로고
    • Characterization of a high activity carbonic anhydrase isozyme purified from erythrocytes of Salmo gairdneri
    • G.E.Hall, R.Schraer. Characterization of a high activity carbonic anhydrase isozyme purified from erythrocytes of Salmo gairdneri. Comp Biochem Physiol B 1983;75:81–92
    • (1983) Comp Biochem Physiol B , vol.75 , pp. 81-92
    • Hall, G.E.1    Schraer, R.2
  • 53
    • 0021923776 scopus 로고
    • Rapid ion-exchange chromatography for preparative separation of proteins. Application to porcine and bovine carbonic anhydrases
    • N.Bergenhem, U.Carlsson, K.Klasson. Rapid ion-exchange chromatography for preparative separation of proteins. Application to porcine and bovine carbonic anhydrases. J Chromatogr 1985;319:59–65
    • (1985) J Chromatogr , vol.319 , pp. 59-65
    • Bergenhem, N.1    Carlsson, U.2    Klasson, K.3
  • 54
    • 0003165989 scopus 로고
    • Carbonic anhydrase of Chlamydomonas: purification and studies on its induction using antiserum against Chlamydomonas carbonic anhydrase
    • S.Y.Yang, M.Tsuzuki, S.Miyachi. Carbonic anhydrase of Chlamydomonas: purification and studies on its induction using antiserum against Chlamydomonas carbonic anhydrase. Plant Cell Physiol 1985;26:25–34
    • (1985) Plant Cell Physiol , vol.26 , pp. 25-34
    • Yang, S.Y.1    Tsuzuki, M.2    Miyachi, S.3
  • 55
    • 0025762220 scopus 로고
    • Purification of carbonic anhydrase isoenzymes by high-performance affinity chromatography and hydrophobic interaction chromatography
    • H.Abou-Rebyeh, D.Josić, K.Gottschall,. Purification of carbonic anhydrase isoenzymes by high-performance affinity chromatography and hydrophobic interaction chromatography. J Chromatogr 1991;566:351–9
    • (1991) J Chromatogr , vol.566 , pp. 351-359
    • Abou-Rebyeh, H.1    Josić, D.2    Gottschall, K.3
  • 56
    • 0030220473 scopus 로고    scopus 로고
    • A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand
    • A.M.Schmidt, H.N.Müller, A.Skerra. A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand. Chem Biol 1996;3:645–53
    • (1996) Chem Biol , vol.3 , pp. 645-653
    • Schmidt, A.M.1    Müller, H.N.2    Skerra, A.3
  • 57
    • 0031281454 scopus 로고    scopus 로고
    • A different structural feature for carbonic anhydrases in human erythrocytes
    • N.Demir, Y.Demir, E.Bakan,. A different structural feature for carbonic anhydrases in human erythrocytes. Prep Biochem Biotechnol 1997;27:279–87
    • (1997) Prep Biochem Biotechnol , vol.27 , pp. 279-287
    • Demir, N.1    Demir, Y.2    Bakan, E.3
  • 58
    • 0032546598 scopus 로고    scopus 로고
    • Molecular characterization of the human carbonic anhydrase-related protein (HCA-RP VIII)
    • N.C.Bergenhem, M.Hallberg, S.Wisén. Molecular characterization of the human carbonic anhydrase-related protein (HCA-RP VIII). Biochim Biophys Acta 1998;1384:294–8
    • (1998) Biochim Biophys Acta , vol.1384 , pp. 294-298
    • Bergenhem, N.C.1    Hallberg, M.2    Wisén, S.3
  • 60
    • 0034619277 scopus 로고    scopus 로고
    • - anion exchanger binding site to the amino-terminal region of carbonic anhydrase II
    • - anion exchanger binding site to the amino-terminal region of carbonic anhydrase II. Biochemistry 2000;39:13344–9
    • (2000) Biochemistry , vol.39 , pp. 13344-13349
    • Vince, J.W.1    Carlsson, U.2    Reithmeier, R.A.3
  • 61
    • 0027389744 scopus 로고
    • Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis
    • L.G.Mårtensson, B.H.Jonsson, P.O.Freskgård,. Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis. Biochemistry 1993;32:224–31
    • (1993) Biochemistry , vol.32 , pp. 224-231
    • Mårtensson, L.G.1    Jonsson, B.H.2    Freskgård, P.O.3
  • 62
    • 0034998819 scopus 로고    scopus 로고
    • Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II
    • M.Persson, J.R.Harbridge, P.Hammarström,. Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II. Biophys J 2001;80:2886–97
    • (2001) Biophys J , vol.80 , pp. 2886-2897
    • Persson, M.1    Harbridge, J.R.2    Hammarström, P.3
  • 63
    • 0035024240 scopus 로고    scopus 로고
    • Characterisation of carbonic anhydrase in Plasmodium falciparum
    • S.R.Krungkrai, N.Suraveratum, S.Rochanakij,. Characterisation of carbonic anhydrase in Plasmodium falciparum. Int J Parasitol 2001;31:661–8
    • (2001) Int J Parasitol , vol.31 , pp. 661-668
    • Krungkrai, S.R.1    Suraveratum, N.2    Rochanakij, S.3
  • 65
    • 0035543096 scopus 로고    scopus 로고
    • Cytosolic and non-cytosolic carbonic anhydrase enzymes from bovine leukocytes
    • Y.Demir, N.Demir, A.Alayli. Cytosolic and non-cytosolic carbonic anhydrase enzymes from bovine leukocytes. Prep Biochem Biotechnol 2001;31:421–31
    • (2001) Prep Biochem Biotechnol , vol.31 , pp. 421-431
    • Demir, Y.1    Demir, N.2    Alayli, A.3
  • 66
    • 3543097391 scopus 로고    scopus 로고
    • A new method for purification of carbonic anhydrase isozymes by affinity chromatography
    • O.Ozensoy, O.Arslan, S.Sinan. A new method for purification of carbonic anhydrase isozymes by affinity chromatography. Biochemistry (Mosc) 2004;69:216–19
    • (2004) Biochemistry (Mosc) , vol.69 , pp. 216-219
    • Ozensoy, O.1    Arslan, O.2    Sinan, S.3
  • 67
    • 0035437677 scopus 로고    scopus 로고
    • Inhibition of bovine carbonic anhydrase by new sulfonamide compounds
    • O.Arslan. Inhibition of bovine carbonic anhydrase by new sulfonamide compounds. Biochemistry (Mosc) 2001;66:982–13
    • (2001) Biochemistry (Mosc) , vol.66 , pp. 913-982
    • Arslan, O.1
  • 68
    • 17144366241 scopus 로고    scopus 로고
    • Purification and characterization of carbonic anhydrase from bovine stomach and effects of some known inhibitors on enzyme activity
    • Y.Demir, H.Nadaroğlu, N.Demir. Purification and characterization of carbonic anhydrase from bovine stomach and effects of some known inhibitors on enzyme activity. J Enzyme Inhib Med Chem 2005;20:75–80
    • (2005) J Enzyme Inhib Med Chem , vol.20 , pp. 75-80
    • Demir, Y.1    Nadaroğlu, H.2    Demir, N.3
  • 69
    • 58949100446 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Cloning, characterization and inhibition studies of the cytosolic isozyme III with anions
    • I.Nishimori, T.Minakuchi, S.Onishi,. Carbonic anhydrase inhibitors. Cloning, characterization and inhibition studies of the cytosolic isozyme III with anions. J Enzyme Inhib Med Chem 2009;24:70–6
    • (2009) J Enzyme Inhib Med Chem , vol.24 , pp. 70-76
    • Nishimori, I.1    Minakuchi, T.2    Onishi, S.3
  • 70
    • 33847756026 scopus 로고    scopus 로고
    • Evidence against a direct interaction between intracellular carbonic anhydrase II and pure C-terminal domains of SLC4 bicarbonate transporters
    • P.M.Piermarini, E.Y.Kim, W.F.Boron. Evidence against a direct interaction between intracellular carbonic anhydrase II and pure C-terminal domains of SLC4 bicarbonate transporters. J Biol Chem 2007;282:1409–21
    • (2007) J Biol Chem , vol.282 , pp. 1409-1421
    • Piermarini, P.M.1    Kim, E.Y.2    Boron, W.F.3
  • 71
    • 84860251805 scopus 로고    scopus 로고
    • Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide
    • J.da Costa Ores, L.Sala, G.P.Cerveira,. Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide. Chemosphere 2012;88:255–9
    • (2012) Chemosphere , vol.88 , pp. 255-259
    • da Costa Ores, J.1    Sala, L.2    Cerveira, G.P.3
  • 72
    • 84884744406 scopus 로고    scopus 로고
    • Immobilization and characterization of carbonic anhydrase purified from E
    • M.Oviya, V.Sukumaran, S.S.Giri. Immobilization and characterization of carbonic anhydrase purified from E. coli MO1 and its influence on CO2 sequestration. World J Microbiol Biotechnol 2013;29:1813–20
    • (2013) World J Microbiol Biotechnol , vol.29 , pp. 1813-1820
    • Oviya, M.1    Sukumaran, V.2    Giri, S.S.3
  • 73
    • 84896142488 scopus 로고    scopus 로고
    • Molecularly imprinted cryogels for carbonic anhydrase purification from bovine erythrocyte
    • M.Uygun, A.A.Karagözler, A.Denizli. Molecularly imprinted cryogels for carbonic anhydrase purification from bovine erythrocyte. Artif Cells Nanomed Biotechnol 2014;42:128–37
    • (2014) Artif Cells Nanomed Biotechnol , vol.42 , pp. 128-137
    • Uygun, M.1    Karagözler, A.A.2    Denizli, A.3
  • 74
    • 84901941588 scopus 로고    scopus 로고
    • Surface histidine mutations for the metal affinity purification of a β-carbonic anhydrase
    • K.M.Hoffmann, K.M.Wood, A.D.Labrum,. Surface histidine mutations for the metal affinity purification of a β-carbonic anhydrase. Anal Biochem 2014;458:66–8
    • (2014) Anal Biochem , vol.458 , pp. 66-68
    • Hoffmann, K.M.1    Wood, K.M.2    Labrum, A.D.3
  • 75
    • 84926619275 scopus 로고    scopus 로고
    • A new affinity gel for the purification of α-carbonic anhydrases
    • A.Sahin, S.Isık, O.Arslan,. A new affinity gel for the purification of α-carbonic anhydrases. J Enzyme Inhib Med Chem 2015;30:224–8
    • (2015) J Enzyme Inhib Med Chem , vol.30 , pp. 224-228
    • Sahin, A.1    Isık, S.2    Arslan, O.3
  • 76
    • 84926487846 scopus 로고    scopus 로고
    • Synthesis of a novel affinity gel for the purification of carbonic anhydrases
    • M.Bozdag, S.Isik, S.Beyaztas,. Synthesis of a novel affinity gel for the purification of carbonic anhydrases. J Enzyme Inhib Med Chem 2015;30:240–4
    • (2015) J Enzyme Inhib Med Chem , vol.30 , pp. 240-244
    • Bozdag, M.1    Isik, S.2    Beyaztas, S.3
  • 77
    • 80053563164 scopus 로고    scopus 로고
    • Interfering with pH regulation in tumours as a therapeutic strategy
    • D.Neri, C.T.Supuran. Interfering with pH regulation in tumours as a therapeutic strategy. Nature Rev Drug Discovery 2011;10:767−77
    • (2011) Nature Rev Drug Discovery , vol.10 , pp. 767
    • Neri, D.1    Supuran, C.T.2
  • 78
    • 84900825323 scopus 로고    scopus 로고
    • Sulfa and trimethoprim-like drugs-antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors
    • C.Capasso, C.T.Supuran. Sulfa and trimethoprim-like drugs-antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors. J Enzyme Inhib Med Chem 2014;29:379–87
    • (2014) J Enzyme Inhib Med Chem , vol.29 , pp. 379-387
    • Capasso, C.1    Supuran, C.T.2
  • 79
    • 84878551753 scopus 로고    scopus 로고
    • Carbonic anhydrase III: a neglected isozyme is stepping into the limelight
    • A.K.Harju, F.Bootorabi, M.Kuuslahti,. Carbonic anhydrase III: a neglected isozyme is stepping into the limelight. J Enzyme Inhib Med Chem 2013;28:231–9
    • (2013) J Enzyme Inhib Med Chem , vol.28 , pp. 231-239
    • Harju, A.K.1    Bootorabi, F.2    Kuuslahti, M.3
  • 80
    • 84855366173 scopus 로고    scopus 로고
    • α-Carbonic anhydrases are sulfatases with cyclic diol monosulfate esters
    • H.Çavdar, D.Ekinci, O.Talaz,. α-Carbonic anhydrases are sulfatases with cyclic diol monosulfate esters. J Enzyme Inhib Med Chem 2012;27:148–54
    • (2012) J Enzyme Inhib Med Chem , vol.27 , pp. 148-154
    • Çavdar, H.1    Ekinci, D.2    Talaz, O.3
  • 81
    • 84904337326 scopus 로고    scopus 로고
    • Inhibition of mammalian carbonic anhydrases I-XIV with grayanotoxin III: solution and in silico studies
    • S.Durdagi, G.Scozzafava, D.Vullo,. Inhibition of mammalian carbonic anhydrases I-XIV with grayanotoxin III: solution and in silico studies. J Enzyme Inhib Med Chem 2014;29:469–75
    • (2014) J Enzyme Inhib Med Chem , vol.29 , pp. 469-475
    • Durdagi, S.1    Scozzafava, G.2    Vullo, D.3
  • 82
    • 84904300213 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Phenols incorporating 2- or 3-pyridyl- ethenylcarbonyl and tertiary amine moieties strongly inhibit Saccharomyces cerevisiaeβ-carbonic anhydrase
    • S.Bilginer, E.Unluer, H.I.Gul,. Carbonic anhydrase inhibitors. Phenols incorporating 2- or 3-pyridyl- ethenylcarbonyl and tertiary amine moieties strongly inhibit Saccharomyces cerevisiaeβ-carbonic anhydrase. J Enzyme Inhib Med Chem 2014;29:495–9
    • (2014) J Enzyme Inhib Med Chem , vol.29 , pp. 495-499
    • Bilginer, S.1    Unluer, E.2    Gul, H.I.3
  • 84
    • 84855408335 scopus 로고    scopus 로고
    • A new approach to antiglaucoma drugs: carbonic anhydrase inhibitors with or without NO donating moieties. Mechanism of action and preliminary pharmacology
    • F.Fabrizi, F.Mincione, T.Somma,. A new approach to antiglaucoma drugs: carbonic anhydrase inhibitors with or without NO donating moieties. Mechanism of action and preliminary pharmacology. J Enzyme Inhib Med Chem 2012;27:138–47
    • (2012) J Enzyme Inhib Med Chem , vol.27 , pp. 138-147
    • Fabrizi, F.1    Mincione, F.2    Somma, T.3
  • 85
    • 84855492167 scopus 로고    scopus 로고
    • Novel therapies for glaucoma: a patent review 2007-2011
    • F.Carta, C.T.Supuran, A.Scozzafava. Novel therapies for glaucoma: a patent review 2007-2011. Expert Opin Ther Pat 2012;22:79–88
    • (2012) Expert Opin Ther Pat , vol.22 , pp. 79-88
    • Carta, F.1    Supuran, C.T.2    Scozzafava, A.3
  • 86
    • 84878083885 scopus 로고    scopus 로고
    • Antiglaucoma carbonic anhydrase inhibitors: a patent review
    • E.Masini, F.Carta, A.Scozzafava,. Antiglaucoma carbonic anhydrase inhibitors: a patent review. Expert Opin Ther Pat 2013;23:705–16
    • (2013) Expert Opin Ther Pat , vol.23 , pp. 705-716
    • Masini, E.1    Carta, F.2    Scozzafava, A.3
  • 87
    • 84890292269 scopus 로고    scopus 로고
    • Three new aromatic sulfonamide inhibitors of carbonic anhydrases I, II, IV and XII
    • C.T.Supuran, A.Maresca, F.Gregáň,. Three new aromatic sulfonamide inhibitors of carbonic anhydrases I, II, IV and XII. J Enzyme Inhib Med Chem 2013;28:289–93
    • (2013) J Enzyme Inhib Med Chem , vol.28 , pp. 289-293
    • Supuran, C.T.1    Maresca, A.2    Gregáň, F.3
  • 88
    • 84879037030 scopus 로고    scopus 로고
    • Secondary/tertiary benzenesulfonamides with inhibitory action against the cytosolic human carbonic anhydrase isoforms I and II
    • C.Alp, A.Maresca, N.A.Alp,. Secondary/tertiary benzenesulfonamides with inhibitory action against the cytosolic human carbonic anhydrase isoforms I and II. J Enzyme Inhib Med Chem 2013;28:294–8
    • (2013) J Enzyme Inhib Med Chem , vol.28 , pp. 294-298
    • Alp, C.1    Maresca, A.2    Alp, N.A.3
  • 89
    • 84878067755 scopus 로고    scopus 로고
    • Anticancer carbonic anhydrase inhibitors: a patent review (2008-2013)
    • S.M.Monti, C.T.Supuran, G.De Simone. Anticancer carbonic anhydrase inhibitors: a patent review (2008-2013). Expert Opin Ther Pat 2013;23:737–49
    • (2013) Expert Opin Ther Pat , vol.23 , pp. 737-749
    • Monti, S.M.1    Supuran, C.T.2    De Simone, G.3
  • 90
    • 66549090944 scopus 로고    scopus 로고
    • Taking advantage of tumor cell adaptations to hypoxia for developing new tumor markers and treatment strategies
    • P.Ebbesen, E.O.Pettersen, T.A.Gorr,. Taking advantage of tumor cell adaptations to hypoxia for developing new tumor markers and treatment strategies. J Enzyme Inhib Med Chem 2009;24:1–39
    • (2009) J Enzyme Inhib Med Chem , vol.24 , pp. 1-39
    • Ebbesen, P.1    Pettersen, E.O.2    Gorr, T.A.3
  • 91
    • 84878072961 scopus 로고    scopus 로고
    • Diuretics with carbonic anhydrase inhibitory action: a patent and literature review (2005-2013)
    • F.Carta, C.T.Supuran. Diuretics with carbonic anhydrase inhibitory action: a patent and literature review (2005-2013). Expert Opin Ther Pat 2013;23:681–91
    • (2013) Expert Opin Ther Pat , vol.23 , pp. 681-691
    • Carta, F.1    Supuran, C.T.2
  • 92
    • 84858966345 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors as emerging drugs for the treatment of obesity
    • C.T.Supuran. Carbonic anhydrase inhibitors as emerging drugs for the treatment of obesity. Expert Opin Emerg Drugs 2012;17:11–15
    • (2012) Expert Opin Emerg Drugs , vol.17 , pp. 11-15
    • Supuran, C.T.1
  • 93
    • 84878062801 scopus 로고    scopus 로고
    • Antiobesity carbonic anhydrase inhibitors: a literature and patent review
    • A.Scozzafava, C.T.Supuran, F.Carta. Antiobesity carbonic anhydrase inhibitors: a literature and patent review. Expert Opin Ther Pat 2013;23:725–35
    • (2013) Expert Opin Ther Pat , vol.23 , pp. 725-735
    • Scozzafava, A.1    Supuran, C.T.2    Carta, F.3
  • 94
    • 84878041301 scopus 로고    scopus 로고
    • Antiinfective carbonic anhydrase inhibitors: a patent and literature review
    • C.Capasso, C.T.Supuran. Antiinfective carbonic anhydrase inhibitors: a patent and literature review. Expert Opin Ther Pat 2013;23:693−704
    • (2013) Expert Opin Ther Pat , vol.23 , pp. 693
    • Capasso, C.1    Supuran, C.T.2
  • 95
    • 84937393508 scopus 로고    scopus 로고
    • Cloning, characterization and anion inhibition study of a β-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans
    • N.Dedeoglu, V.De Luca, S.Isik,. Cloning, characterization and anion inhibition study of a β-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans. Bioorg Med Chem 2015;23:2995–3001
    • (2015) Bioorg Med Chem , vol.23 , pp. 2995-3001
    • Dedeoglu, N.1    De Luca, V.2    Isik, S.3


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