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Volumn 66, Issue 1, 2005, Pages 41-49

Purification of cynarases from artichoke (Cynara scolymus L.): Enzymatic properties of cynarase A

Author keywords

Artichoke; Aspartic endopeptidase; Cynara scolymus L.; Proteinase purification; Spectroscopy; Steady state kinetics

Indexed keywords

CYNARASE; CYNARASE A; CYNARASE B; PROTEINASE; UNCLASSIFIED DRUG;

EID: 11844306589     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2004.10.005     Document Type: Article
Times cited : (67)

References (30)
  • 2
    • 0036838183 scopus 로고    scopus 로고
    • Determination of proteolytic activity in different milk systems
    • S. Bendicho, G. Martí, T. Hernández, and O. Martín Determination of proteolytic activity in different milk systems Food Chem. 79 2002 245 249
    • (2002) Food Chem. , vol.79 , pp. 245-249
    • Bendicho, S.1    Martí, G.2    Hernández, T.3    Martín, O.4
  • 3
    • 0010590129 scopus 로고
    • Influence of calcium chloride on the chymosin-initiated coagulation of casein micelles
    • N.A. Bringe, and J.E. Kinsella Influence of calcium chloride on the chymosin-initiated coagulation of casein micelles J. Dairy Res. 53 1986 371 379
    • (1986) J. Dairy Res. , vol.53 , pp. 371-379
    • Bringe, N.A.1    Kinsella, J.E.2
  • 4
    • 0029129455 scopus 로고
    • Aspartic proteinases (cyprosins) from Cynara cardunculus spp. flavescens cv. cardoon; Purification, characterisation, and tissue-specific expression
    • P.E. Brodelius, M.C. Cordeiro, and M.S. Pais Aspartic proteinases (cyprosins) from Cynara cardunculus spp. flavescens cv. cardoon; purification, characterisation, and tissue-specific expression Adv. Exp. Med. Biol. 362 1995 255 266
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 255-266
    • Brodelius, P.E.1    Cordeiro, M.C.2    Pais, M.S.3
  • 5
    • 0032054231 scopus 로고    scopus 로고
    • Chymosin and aspartic proteinases
    • S. Chitipinityol, and M.J.C. Crabbe Chymosin and aspartic proteinases Food Chem. 61 1998 395 418
    • (1998) Food Chem. , vol.61 , pp. 395-418
    • Chitipinityol, S.1    Crabbe, M.J.C.2
  • 6
    • 0031944728 scopus 로고    scopus 로고
    • Substrate specificity and molecular modelling of aspartic proteinases (cyprosins) from flowers of Cynara cardunculus subsp. flavescens cv. Cardoon
    • M. Cordeiro, T. Lowther, B.M. Dunn, K. Guruprasad, T. Blundell, M.S. Pais, and P.E. Brodelius Substrate specificity and molecular modelling of aspartic proteinases (cyprosins) from flowers of Cynara cardunculus subsp. flavescens cv. Cardoon Adv. Exp. Med. Biol. 436 1998 473 479
    • (1998) Adv. Exp. Med. Biol. , vol.436 , pp. 473-479
    • Cordeiro, M.1    Lowther, T.2    Dunn, B.M.3    Guruprasad, K.4    Blundell, T.5    Pais, M.S.6    Brodelius, P.E.7
  • 8
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • B.M. Dunn Structure and mechanism of the pepsin-like family of aspartic peptidases Chem. Rev. 102 2002 4431 4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 9
    • 0021415850 scopus 로고
    • The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subsite preferences
    • B.M. Dunn, B. Kammerman, and K.R. McCurry The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: design of a substrate based on subsite preferences Anal. Biochem. 138 1984 68 73
    • (1984) Anal. Biochem. , vol.138 , pp. 68-73
    • Dunn, B.M.1    Kammerman, B.2    McCurry, K.R.3
  • 10
    • 0034763148 scopus 로고    scopus 로고
    • Mathematical modelling of the formation of rennet-induced gels by plant coagulants and chymosin
    • C.L.C. Esteves, J.A. Lucey, and E.M.V. Pires Mathematical modelling of the formation of rennet-induced gels by plant coagulants and chymosin J. Dairy Res. 68 2001 499 510
    • (2001) J. Dairy Res. , vol.68 , pp. 499-510
    • Esteves, C.L.C.1    Lucey, J.A.2    Pires, E.M.V.3
  • 11
    • 0033600810 scopus 로고    scopus 로고
    • Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp- containing aspartic proteinase from the flowers of Cynara cardunculus L
    • C. Frazao, I. Bento, J. Costa, C.M. Soares, P. Verissimo, C. Faro, E. Pires, J. Cooper, and M.A. Carrondo Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L J. Biol. Chem. 274 1999 27694 27701
    • (1999) J. Biol. Chem. , vol.274 , pp. 27694-27701
    • Frazao, C.1    Bento, I.2    Costa, J.3    Soares, C.M.4    Verissimo, P.5    Faro, C.6    Pires, E.7    Cooper, J.8    Carrondo, M.A.9
  • 13
    • 0028672474 scopus 로고
    • Use of least-squares techniques in biochemistry
    • M.L. Johnson Use of least-squares techniques in biochemistry Methods Enzymol. 240 1994 1 22
    • (1994) Methods Enzymol. , vol.240 , pp. 1-22
    • Johnson, M.L.1
  • 14
    • 0034327782 scopus 로고    scopus 로고
    • High-throughput screening of enzyme inhibitors: Simultaneous determination of tight-binding inhibition constants and enzyme concentration
    • P. Kuzmic, K.C. Elrod, L.M. Cregar, S. Sideris, R. Rai, and J.W. Janc High-throughput screening of enzyme inhibitors: simultaneous determination of tight-binding inhibition constants and enzyme concentration Anal. Biochem. 286 2000 45 50
    • (2000) Anal. Biochem. , vol.286 , pp. 45-50
    • Kuzmic, P.1    Elrod, K.C.2    Cregar, L.M.3    Sideris, S.4    Rai, R.5    Janc, J.W.6
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0020440235 scopus 로고
    • Regression analysis, experimental error an statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models
    • B. Mannervik Regression analysis, experimental error an statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models Methods Enzymol. 87 1982 370 390
    • (1982) Methods Enzymol. , vol.87 , pp. 370-390
    • Mannervik, B.1
  • 17
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • D.W. Marquardt An algorithm for least-squares estimation of nonlinear parameters J. Soc. Ind. Appl. Math. 11 1963 431 441
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 18
    • 0010627796 scopus 로고
    • A mathematical model for the description of chymosin action on casein micelles
    • U. Merin, H. Talpaz, and S. Fishman A mathematical model for the description of chymosin action on casein micelles J. Dairy Res. 56 1989 76 86
    • (1989) J. Dairy Res. , vol.56 , pp. 76-86
    • Merin, U.1    Talpaz, H.2    Fishman, S.3
  • 19
    • 0000416960 scopus 로고
    • Hydrolysis of α-lactalbumin by chymosin and pepsin: Effect of conformation and pH
    • G. Miranda, G. Hazé, P. Scanff, and J.P. Pélissier Hydrolysis of α-lactalbumin by chymosin and pepsin: effect of conformation and pH Lait 69 1989 451 459
    • (1989) Lait , vol.69 , pp. 451-459
    • Miranda, G.1    Hazé, G.2    Scanff, P.3    Pélissier, J.P.4
  • 20
    • 0000708150 scopus 로고
    • Interaction of calcium, pH, temperature and chymosin during milk coagulation
    • L.M. Okigbo, G.H. Richardson, R.J. Brown, and C.A. Ernstrom Interaction of calcium, pH, temperature and chymosin during milk coagulation J. Dairy Res. 68 1985 3135 3142
    • (1985) J. Dairy Res. , vol.68 , pp. 3135-3142
    • Okigbo, L.M.1    Richardson, G.H.2    Brown, R.J.3    Ernstrom, C.A.4
  • 21
    • 0031257393 scopus 로고    scopus 로고
    • Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L
    • M. Ramalho-Santos, J. Pissarra, P. Veríssimo, S. Pereira, R. Salema, E. Pires, and C.J. Faro Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L Planta 203 1997 204 212
    • (1997) Planta , vol.203 , pp. 204-212
    • Ramalho-Santos, M.1    Pissarra, J.2    Veríssimo, P.3    Pereira, S.4    Salema, R.5    Pires, E.6    Faro, C.J.7
  • 22
    • 0018956026 scopus 로고
    • Mechanism of inhibition of pepsin by pepstatin - Effect of inhibitor structure on dissociation-constant and time-dependent inhibition
    • D.H. Rich, and E.T.O. Sun Mechanism of inhibition of pepsin by pepstatin - effect of inhibitor structure on dissociation-constant and time-dependent inhibition Biochem. Pharmacol. 29 1980 2205 2212
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 2205-2212
    • Rich, D.H.1    Sun, E.T.O.2
  • 23
    • 0037413445 scopus 로고    scopus 로고
    • Cardosin a as a model aspartic proteinase for the study of organic solvents effects. An overview on catalytic and structural aspects
    • A.C. Sarmento, C. Oliveira, E. Pires, P. Halling, and M. Barros Cardosin A as a model aspartic proteinase for the study of organic solvents effects. An overview on catalytic and structural aspects J. Mol. Catal. B: Enzym. 21 2003 19 23
    • (2003) J. Mol. Catal. B: Enzym. , vol.21 , pp. 19-23
    • Sarmento, A.C.1    Oliveira, C.2    Pires, E.3    Halling, P.4    Barros, M.5
  • 24
    • 0036322991 scopus 로고    scopus 로고
    • Hydrolysis of caseins by extracts of Cynara cardunculus precipited by ammonium sulphate
    • S.V. Silva, R.M. Barros, and F.X. Malcaa Hydrolysis of caseins by extracts of Cynara cardunculus precipited by ammonium sulphate J. Food Sci. 67 2002 1746 1751
    • (2002) J. Food Sci. , vol.67 , pp. 1746-1751
    • Silva, S.V.1    Barros, R.M.2    Malcaa, F.X.3
  • 25
    • 0034870511 scopus 로고    scopus 로고
    • Advances in the study of proteolysis during cheese ripening
    • M.J. Sousa, Y. Ardo, and P.L.H. McSweeney Advances in the study of proteolysis during cheese ripening Int. Dairy J. 11 2001 327 345
    • (2001) Int. Dairy J. , vol.11 , pp. 327-345
    • Sousa, M.J.1    Ardo, Y.2    McSweeney, P.L.H.3
  • 26
    • 11844250408 scopus 로고    scopus 로고
    • SPSS Inc., Chicago, IL
    • SPSS Inc., 2003. Sigma Plot. SPSS Inc., Chicago, IL
    • (2003) Sigma Plot
  • 27
    • 0028924136 scopus 로고
    • Kinetics of slow and tight-binding inhibitors
    • D.L. Purich Academic Press New York
    • S.E. Szedlacsek, and R.G. Duggleby Kinetics of slow and tight-binding inhibitors D.L. Purich Enzyme Kinetics and Mechanism, Part D 1995 Academic Press New York 144 180
    • (1995) Enzyme Kinetics and Mechanism, Part D , pp. 144-180
    • Szedlacsek, S.E.1    Duggleby, R.G.2
  • 28
    • 0030060726 scopus 로고    scopus 로고
    • Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L
    • P. Verissimo, C. Faro, A.J. Moir, Y. Lin, J. Tang, and E. Pires Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L Eur. J. Biochem. 235 1996 762 768
    • (1996) Eur. J. Biochem. , vol.235 , pp. 762-768
    • Verissimo, P.1    Faro, C.2    Moir, A.J.3    Lin, Y.4    Tang, J.5    Pires, E.6
  • 29
    • 0031919032 scopus 로고    scopus 로고
    • A comparative study on the aspartic proteinases from different species of Cynara
    • P. Verissimo, M. Ramalho-Santos, C. Faro, and E. Pires A comparative study on the aspartic proteinases from different species of Cynara Aspartic Proteinases 436 1998 459 463
    • (1998) Aspartic Proteinases , vol.436 , pp. 459-463
    • Verissimo, P.1    Ramalho-Santos, M.2    Faro, C.3    Pires, E.4
  • 30
    • 0033546412 scopus 로고    scopus 로고
    • Processing, activity, and inhibition of recombinant cyprosin, an aspartic proteinase from cardoon (Cynara cardunculus)
    • P.C. White, M.C. Cordeiro, D. Arnold, P.E. Brodelius, and J. Kay Processing, activity, and inhibition of recombinant cyprosin, an aspartic proteinase from cardoon (Cynara cardunculus) J. Biol. Chem. 274 1999 16685 16693
    • (1999) J. Biol. Chem. , vol.274 , pp. 16685-16693
    • White, P.C.1    Cordeiro, M.C.2    Arnold, D.3    Brodelius, P.E.4    Kay, J.5


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