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Volumn 69, Issue 3, 2008, Pages 647-655

An unusual thermostable aspartic protease from the latex of Ficus racemosa (L.)

Author keywords

Aspartic protease; Endopeptidases; Ficin; Ficus racemosa; Moraceae; Plant proteases

Indexed keywords

ASPARTIC PROTEINASE; LATEX; PROTEIN; PROTEINASE INHIBITOR;

EID: 38349120529     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2007.09.003     Document Type: Article
Times cited : (66)

References (33)
  • 1
    • 0000975925 scopus 로고
    • Aspartic proteinase from wheat seeds: Isolation, properties and action on gliadin
    • Belozersky M.A., Sarbakanova S.T., and Dunaevsky Y.E. Aspartic proteinase from wheat seeds: Isolation, properties and action on gliadin. Planta 177 (1989) 321-326
    • (1989) Planta , vol.177 , pp. 321-326
    • Belozersky, M.A.1    Sarbakanova, S.T.2    Dunaevsky, Y.E.3
  • 2
    • 0036838183 scopus 로고    scopus 로고
    • Determination of proteolytic activity in different milk systems
    • Bendicho S., Marti G., Hernandez T., and Martin O. 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    Marti, G.2    Hernandez, T.3    Martin, O.4
  • 3
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interaction of plants with other organisms
    • Dalling M.J. (Ed), CRC Press, Boca Raton, FL
    • Boller T. Roles of proteolytic enzymes in interaction of plants with other organisms. In: Dalling M.J. (Ed). Plant Proteolytic Enzymes vol. 1 (1986), CRC Press, Boca Raton, FL 67-96
    • (1986) Plant Proteolytic Enzymes , vol.1 , pp. 67-96
    • Boller, T.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0141784573 scopus 로고
    • Proteases of higher plants. General features, physiological roles and applications
    • Caffini N.O., Lopez L.M.I., Natalucci C.L., and Priolo N.S. Proteases of higher plants. General features, physiological roles and applications. Acta. Farm. Bonaerense 7 (1988) 195-213
    • (1988) Acta. Farm. Bonaerense , vol.7 , pp. 195-213
    • Caffini, N.O.1    Lopez, L.M.I.2    Natalucci, C.L.3    Priolo, N.S.4
  • 6
    • 0033711401 scopus 로고    scopus 로고
    • Purification, cloning and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa
    • Domingos A., Cardoso P.C., Xue Z., Clemente A., Brodelius P.E., and Pais M.S. Purification, cloning and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa. Eur. J. Biochem. 267 (2000) 6824-6831
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6824-6831
    • Domingos, A.1    Cardoso, P.C.2    Xue, Z.3    Clemente, A.4    Brodelius, P.E.5    Pais, M.S.6
  • 7
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink M.R., and Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114 (1981) 199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 8
    • 0014223589 scopus 로고
    • Studies on ficin I. Its isolation and characterization
    • Englund P.T., King T.P., Craig L.C., and Walti A. Studies on ficin I. Its isolation and characterization. Biochemistry 7 (1968) 163-175
    • (1968) Biochemistry , vol.7 , pp. 163-175
    • Englund, P.T.1    King, T.P.2    Craig, L.C.3    Walti, A.4
  • 9
    • 0031014713 scopus 로고    scopus 로고
    • Activity staining of protein inhibitors of proteases on gelatin-containing polyacrylamide gel electrophoresis
    • Felicioli R., Garzelli B., Vaccari L., Melfi D., and Balestreri E. Activity staining of protein inhibitors of proteases on gelatin-containing polyacrylamide gel electrophoresis. Anal. Biochem. 244 (1997) 176-179
    • (1997) Anal. Biochem. , vol.244 , pp. 176-179
    • Felicioli, R.1    Garzelli, B.2    Vaccari, L.3    Melfi, D.4    Balestreri, E.5
  • 10
    • 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
    • Frazao C., Bento I., Costa J., Soares C.M., Verissimo P., Faro C., Pires E., Cooper J., and Carrondo M.A. 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
  • 11
    • 0016914760 scopus 로고
    • Mechanism of the catalytic action of pepsin and related acidic proteases
    • Fruton J.S. Mechanism of the catalytic action of pepsin and related acidic proteases. Adv. Enzymol. 44 (1976) 1-36
    • (1976) Adv. Enzymol. , vol.44 , pp. 1-36
    • Fruton, J.S.1
  • 12
    • 0014939674 scopus 로고
    • Comparative studies on four sulfhydryl endopeptidases (Ficins) of Ficus glabrata latex
    • Jones I.K., and Glazer A.N. Comparative studies on four sulfhydryl endopeptidases (Ficins) of Ficus glabrata latex. J. Biol. Chem. 245 (1970) 2765-2772
    • (1970) J. Biol. Chem. , vol.245 , pp. 2765-2772
    • Jones, I.K.1    Glazer, A.N.2
  • 13
    • 85010612852 scopus 로고    scopus 로고
    • Purification and some properties of a protease from the sarcocarp of musk melon fruit
    • Kaneda M., Yonezawa H., and Uchikoba T. Purification and some properties of a protease from the sarcocarp of musk melon fruit. Biosci. Biotech. Biochem. 61 (1997) 2100-2102
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 2100-2102
    • Kaneda, M.1    Yonezawa, H.2    Uchikoba, T.3
  • 14
    • 0033565640 scopus 로고    scopus 로고
    • Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting
    • Kervinen J., Tobin G.J., Costa J., Waugh D.S., Wlodawer A., and Zdanov A. Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J. 18 (1999) 3947-3955
    • (1999) EMBO J. , vol.18 , pp. 3947-3955
    • Kervinen, J.1    Tobin, G.J.2    Costa, J.3    Waugh, D.S.4    Wlodawer, A.5    Zdanov, A.6
  • 15
    • 0011021887 scopus 로고
    • Purification and characterization of protease Ci, a cytoplasmic metalloendoprotease in Escherichia coli
    • Kim K., Baek S.H., Hong Y., Kang M., Ha D.B., Goldberg A.L., and Chung C.H. Purification and characterization of protease Ci, a cytoplasmic metalloendoprotease in Escherichia coli. J. Biol. Chem. 270 (1995) 29799-29805
    • (1995) J. Biol. Chem. , vol.270 , pp. 29799-29805
    • Kim, K.1    Baek, S.H.2    Hong, Y.3    Kang, M.4    Ha, D.B.5    Goldberg, A.L.6    Chung, C.H.7
  • 16
    • 0016250637 scopus 로고
    • Ficins (EC 3.4.22.3). Purification and characterization of the enzymatic components of the latex of Ficus glabrata
    • Kortt A.A., Hamilton S., Webb E.C., and Zerner B. Ficins (EC 3.4.22.3). Purification and characterization of the enzymatic components of the latex of Ficus glabrata. Biochemistry 13 (1974) 2023-2028
    • (1974) Biochemistry , vol.13 , pp. 2023-2028
    • Kortt, A.A.1    Hamilton, S.2    Webb, E.C.3    Zerner, B.4
  • 17
    • 0000391619 scopus 로고
    • Ficus enzymes II. Properties of the proteolytic enzymes from the latex of Ficus carica variety kodata
    • Kramer D.E., and Whitaker J.R. Ficus enzymes II. Properties of the proteolytic enzymes from the latex of Ficus carica variety kodata. J. Biol. Chem. 239 (1964) 2178-2183
    • (1964) J. Biol. Chem. , vol.239 , pp. 2178-2183
    • Kramer, D.E.1    Whitaker, J.R.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0000656852 scopus 로고
    • Ficin-E, a serine centered protease from Ficus elastica
    • Lynn K.R., and Clevette-Radford N.A. Ficin-E, a serine centered protease from Ficus elastica. Phytochemistry 25 (1986) 1559-1561
    • (1986) Phytochemistry , vol.25 , pp. 1559-1561
    • Lynn, K.R.1    Clevette-Radford, N.A.2
  • 21
    • 0014140406 scopus 로고
    • Purification, partial characterization, and sequence around a reactive sulfhydryl of ficin
    • Metrione R.M., Johnson R.B., and Seng R. Purification, partial characterization, and sequence around a reactive sulfhydryl of ficin. Arch. Biochem. Biophys. 122 (1967) 137-143
    • (1967) Arch. Biochem. Biophys. , vol.122 , pp. 137-143
    • Metrione, R.M.1    Johnson, R.B.2    Seng, R.3
  • 23
    • 5344245485 scopus 로고
    • Effect of proteases on arachin, conarachin I and conarachin II from the peanut (Arachis hypogaea L.)
    • Monteiro P.V., and Prakash V. Effect of proteases on arachin, conarachin I and conarachin II from the peanut (Arachis hypogaea L.). J. Agric. Food Chem. 42 (1994) 268-273
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 268-273
    • Monteiro, P.V.1    Prakash, V.2
  • 24
    • 37049178293 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath H. Evolution of proteolytic enzymes. Science 224 (1984) 350-357
    • (1984) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 25
    • 0032126745 scopus 로고    scopus 로고
    • Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells
    • Runeberg-Roos P., and Saarma M. Phytepsin, a barley vacuolar aspartic proteinase, is highly expressed during autolysis of developing tracheary elements and sieve cells. Plant J. 15 (1998) 139-145
    • (1998) Plant J. , vol.15 , pp. 139-145
    • Runeberg-Roos, P.1    Saarma, M.2
  • 26
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophy. Res. Commun. 22 (1967) 157-162
    • (1967) Biochem. Biophy. Res. Commun. , vol.22 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 27
    • 78651158997 scopus 로고
    • Ficus enzymes I. Separation of the proteolytic enzymes of Ficus carica and Ficus glabrata lattices
    • Sgarbieri V.C., Gupte S.M., Kramer D.E., and Whitaker J.R. Ficus enzymes I. Separation of the proteolytic enzymes of Ficus carica and Ficus glabrata lattices. J. Biol. Chem. 239 (1964) 2170-2177
    • (1964) J. Biol. Chem. , vol.239 , pp. 2170-2177
    • Sgarbieri, V.C.1    Gupte, S.M.2    Kramer, D.E.3    Whitaker, J.R.4
  • 28
    • 11844306589 scopus 로고    scopus 로고
    • Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A
    • Sidarch L., Garcia-Canovas F., Tudela J., and Rodriguez-Lopez J.N. Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A. Phytochemistry 66 (2005) 41-49
    • (2005) Phytochemistry , vol.66 , pp. 41-49
    • Sidarch, L.1    Garcia-Canovas, F.2    Tudela, J.3    Rodriguez-Lopez, J.N.4
  • 29
    • 0034870511 scopus 로고    scopus 로고
    • Advances in the study of proteolysis during cheese ripening
    • Sousa M.J., Ardo Y., and McSweeney P.L.H. 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
  • 30
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. A straight forward fractionation and their characterization
    • Tanh V.H., and Shibasaki K. Major proteins of soybean seeds. A straight forward fractionation and their characterization. J. Agric. Food Chem. 24 (1976) 1117-1121
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 1117-1121
    • Tanh, V.H.1    Shibasaki, K.2
  • 31
    • 38349114375 scopus 로고    scopus 로고
    • Description of enzymes
    • Uhlig H. (Ed), John Wiley & Sons, Inc., New York
    • Uhlig H. Description of enzymes. In: Uhlig H. (Ed). Industrial Enzymes and their Applications (1998), John Wiley & Sons, Inc., New York 146-151
    • (1998) Industrial Enzymes and their Applications , pp. 146-151
    • Uhlig, H.1
  • 32
    • 33746189464 scopus 로고    scopus 로고
    • Highly stable glycosylated serine protease from the medicinal plant Euphorbia milii
    • Yadav S.C., Pande M., and Jagannadham M.V. Highly stable glycosylated serine protease from the medicinal plant Euphorbia milii. Phytochemistry 67 (2006) 1414-1426
    • (2006) Phytochemistry , vol.67 , pp. 1414-1426
    • Yadav, S.C.1    Pande, M.2    Jagannadham, M.V.3
  • 33
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang J.T., Wu C.S.C., and Martinez H.M. Calculation of protein conformation from circular dichroism. Meth. Enzymol. 130 (1986) 208-269
    • (1986) Meth. Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.