메뉴 건너뛰기




Volumn 18, Issue 2, 2000, Pages 133-140

Purification and characterization of macrodontain I, a cysteine peptidase from unripe fruits of Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ANION EXCHANGE CHROMATOGRAPHY; CYSTEINE PEPTIDASE; ENZYME ACTIVITY; ENZYME PURIFICATION; ION EXCHANGE CHROMATOGRAPHY; ISOELECTRIC POINT; MACRODONTAIN I; NUCLEOTIDE SEQUENCE; PH; PROTEINASE; SEQUENCE HOMOLOGY;

EID: 0042446305     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1165     Document Type: Article
Times cited : (50)

References (49)
  • 2
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interactions of plants with other organisms
    • M. J. Dalling. Boca Raton: CRC Press
    • Boller T. Roles of proteolytic enzymes in interactions of plants with other organisms. Dalling M. J. Plant Proteolytic Enzymes. 1986;67-96 CRC Press, Boca Raton.
    • (1986) Plant Proteolytic Enzymes , pp. 67-96
    • Boller, T.1
  • 3
    • 0017219079 scopus 로고
    • Bromelian enzymes
    • Murachi T. Bromelian enzymes. Methods Enzymol. 45:1976;475-485.
    • (1976) Methods Enzymol. , vol.45 , pp. 475-485
    • Murachi, T.1
  • 4
    • 0022087186 scopus 로고
    • Reinvestigation of fractionation and some properties of the proteolytically active components of stem and fruit bromelains
    • Ota S., Muta E., Katahira J., Okamoto Y. Reinvestigation of fractionation and some properties of the proteolytically active components of stem and fruit bromelains. J. Biochem. 98:1985;219-228.
    • (1985) J. Biochem. , vol.98 , pp. 219-228
    • Ota, S.1    Muta, E.2    Katahira, J.3    Okamoto, Y.4
  • 6
    • 0028672814 scopus 로고
    • Pineapple cysteine endopeptidases
    • Rowan A. D., Buttle D. J. Pineapple cysteine endopeptidases. Methods Enzymol. 244:1994;555-568.
    • (1994) Methods Enzymol. , vol.244 , pp. 555-568
    • Rowan, A.D.1    Buttle, D.J.2
  • 7
    • 0030681334 scopus 로고    scopus 로고
    • Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases
    • Lee K., Albee K., Bernasconi R., Edmunds T. Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases. Biochem. J. 327:1997;199-202.
    • (1997) Biochem. J. , vol.327 , pp. 199-202
    • Lee, K.1    Albee, K.2    Bernasconi, R.3    Edmunds, T.4
  • 8
    • 0014309816 scopus 로고
    • Isolation, purification and partial characterization of pinguinain, the proteolytic enzyme from Bromelia pinguin L
    • Toro-Goyco E., Maretzki A., Matos M. L. Isolation, purification and partial characterization of pinguinain, the proteolytic enzyme from Bromelia pinguin L. Arch. Biochem. Biophys. 126:1968;91-104.
    • (1968) Arch. Biochem. Biophys. , vol.126 , pp. 91-104
    • Toro-Goyco, E.1    Maretzki, A.2    Matos, M.L.3
  • 9
    • 0018889777 scopus 로고
    • Structural studies on pinguinain: Changes induced by carboxamidomethylation
    • Toro-Goyco E., Rodríguez-Costas I., Ehrig H. Structural studies on pinguinain: Changes induced by carboxamidomethylation. Biochim. Biophys. Acta. 622:1980;151-159.
    • (1980) Biochim. Biophys. Acta , vol.622 , pp. 151-159
    • Toro-Goyco, E.1    Rodríguez-Costas, I.2    Ehrig, H.3
  • 10
    • 0001900022 scopus 로고
    • Proteinasas de plantas mexicanas. I. Determinación de pesos moleculares de proteinasas cisteínicas por concentración de grupos tioles
    • Cruz M. T., Oliver M. C., Del Castillo L. M., Castañeda-Agulló M. Proteinasas de plantas mexicanas. I. Determinación de pesos moleculares de proteinasas cisteínicas por concentración de grupos tioles. Rev. Latinoamer. Quím. 5:1974;18-25.
    • (1974) Rev. Latinoamer. Quím. , vol.5 , pp. 18-25
    • Cruz, M.T.1    Oliver, M.C.2    Del Castillo, L.M.3    Castañeda-Agulló, M.4
  • 12
    • 0025069044 scopus 로고
    • Subunit structure of karatasin, the proteinase isolated from Bromelia plumieri (karatas)
    • Montes C., Amador M., Cuevas D., Córdoba F. Subunit structure of karatasin, the proteinase isolated from Bromelia plumieri (karatas). Agric. Biol. Chem. 54:1990;17-24.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 17-24
    • Montes, C.1    Amador, M.2    Cuevas, D.3    Córdoba, F.4
  • 14
    • 0030366389 scopus 로고    scopus 로고
    • Macrodontain, a new protease isolated from fruits of Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)
    • Natalucci, C. L., Brullo, A., López, L. M. I., Hilal, R. M., and Caffini, N. O.1996 Macrodontain, a new protease isolated from fruits of Pseudananas macrodontes (Morr.) Harms (Bromeliaceae). J. Food Biochem.19, 443-454.
    • (1996) J. Food Biochem. , vol.19 , pp. 443-454
    • Natalucci, C.L.1    Brullo, A.2    López, L.M.I.3    Hilal, R.M.4    Caffini, N.O.5
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. B. A rapid and sensitive method for the quantitation of micrograms 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.B.1
  • 17
    • 0002006941 scopus 로고
    • Inhibition of proteolytic enzymes
    • R. J. Beynon, & J. S. Bond. Oxford: IRL Press
    • Salvensen G., Nagase H. Inhibition of proteolytic enzymes. Beynon R. J., Bond J. S. Proteolytic Enzymes: A Practical Approach. 1989;83-104 IRL Press, Oxford.
    • (1989) Proteolytic Enzymes: A Practical Approach , pp. 83-104
    • Salvensen, G.1    Nagase, H.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. 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
  • 20
    • 33845471438 scopus 로고
    • Heat-induced interactions between soybean proteins: Preferential association of 11S basic subunits and β-subunits of 7S
    • Utsumi S., Damodaran S., Kinsella J. E. Heat-induced interactions between soybean proteins: Preferential association of 11S basic subunits and β-subunits of 7S. J. Agric. Food Chem. 32:1984;1406-1412.
    • (1984) J. Agric. Food Chem. , vol.32 , pp. 1406-1412
    • Utsumi, S.1    Damodaran, S.2    Kinsella, J.E.3
  • 22
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:1987;10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 24
    • 0024551586 scopus 로고
    • Stem bromelain: Amino acid sequence and implications for weak binding of cystatin
    • Ritonja A., Rowan A. D., Buttle D. J., Rawlings N. D., Turk V., Barrett A. J. Stem bromelain: Amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247:1989;419-424.
    • (1989) FEBS Lett. , vol.247 , pp. 419-424
    • Ritonja, A.1    Rowan, A.D.2    Buttle, D.J.3    Rawlings, N.D.4    Turk, V.5    Barrett, A.J.6
  • 25
    • 0025008745 scopus 로고
    • The amino acid sequence of chymopapain from Carica papaya
    • Watson D. C., Yaguchi M., Lynn K. R. The amino acid sequence of chymopapain from Carica papaya. Biochem. J. 266:1990;75-81.
    • (1990) Biochem. J. , vol.266 , pp. 75-81
    • Watson, D.C.1    Yaguchi, M.2    Lynn, K.R.3
  • 27
    • 0027636376 scopus 로고
    • Isolation and preliminary characterization of the cysteine proteinases from the latex of Carica candamarcensis Hook
    • Walreavens V., Jaziri M., van Beeumen J., Schnek A. G., Kleinschmidt T., Looze Y. Isolation and preliminary characterization of the cysteine proteinases from the latex of Carica candamarcensis Hook. Biol. Chem. Hoppe-Seyler. 374:1993;501-506.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 501-506
    • Walreavens, V.1    Jaziri, M.2    Van Beeumen, J.3    Schnek, A.G.4    Kleinschmidt, T.5    Looze, Y.6
  • 28
    • 0028446499 scopus 로고
    • Primary structure of CC-III, the glycosilated cysteine proteinase from the latex of Carica candamarcensis Hook
    • Jaziri M., Kleinschmidt T., Walreavens V., Schnek A. G., Looze Y. Primary structure of CC-III, the glycosilated cysteine proteinase from the latex of Carica candamarcensis Hook. Biol. Chem. Hoppe-Seyler. 375:1994;379-385.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 379-385
    • Jaziri, M.1    Kleinschmidt, T.2    Walreavens, V.3    Schnek, A.G.4    Looze, Y.5
  • 29
    • 0000024298 scopus 로고
    • Degradation of storage proteins in germinating seeds
    • Shutov A., Vaintraub I. Degradation of storage proteins in germinating seeds. Phytochemistry. 26:1987;1557-1566.
    • (1987) Phytochemistry , vol.26 , pp. 1557-1566
    • Shutov, A.1    Vaintraub, I.2
  • 30
    • 0029951575 scopus 로고    scopus 로고
    • Structure and expression of a developmentally regulated cDNA encoding a cysteine protease (pseudotzain) from Douglas fir
    • Tranbarger T. J., Misra S. Structure and expression of a developmentally regulated cDNA encoding a cysteine protease (pseudotzain) from Douglas fir. Gene. 172:1996;221-226.
    • (1996) Gene , vol.172 , pp. 221-226
    • Tranbarger, T.J.1    Misra, S.2
  • 31
    • 0027274695 scopus 로고
    • Structure and expression of two genes that encode distinct drought-inducible cytsteine proteinases in Arabidopsis thaliana
    • Koizumi M., Yamaguchi-Shinozaki K., Tsuji H., Shinozaki K. Structure and expression of two genes that encode distinct drought-inducible cytsteine proteinases in Arabidopsis thaliana. Gene. 129:1993;175-182.
    • (1993) Gene , vol.129 , pp. 175-182
    • Koizumi, M.1    Yamaguchi-Shinozaki, K.2    Tsuji, H.3    Shinozaki, K.4
  • 32
    • 0028426945 scopus 로고
    • Characterization of a cDNA from Arabidopsis thaliana encoding a potential thiol-protease whose expression is induced independetly by wilting and abscisic acid
    • Williams J., Bulman M., Huttly A., Phillips A., Neill S. Characterization of a cDNA from Arabidopsis thaliana encoding a potential thiol-protease whose expression is induced independetly by wilting and abscisic acid. Plant Mol. Biol. 25:1994;259-270.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 259-270
    • Williams, J.1    Bulman, M.2    Huttly, A.3    Phillips, A.4    Neill, S.5
  • 33
    • 0026095842 scopus 로고
    • Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains)
    • Watanabe H., Abe K., Emori Y, Hosoyama H., Arai S. Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains). J. Biol. Chem. 266:1991;16897-16902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16897-16902
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Arai, S.5
  • 34
    • 0027547387 scopus 로고
    • Circadian expression and induction by wounding of tobacco genes for cysteine proteinase
    • Linthorst H. G., van der Does C., Brederode F. T., Bol J. F. Circadian expression and induction by wounding of tobacco genes for cysteine proteinase. Plant Mol. Biol. 21:1993;685-694.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 685-694
    • Linthorst, H.G.1    Van Der Does, C.2    Brederode, F.T.3    Bol, J.F.4
  • 35
    • 0032189507 scopus 로고    scopus 로고
    • A cysteine endopeptidase with C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosoma, a putative lytic compartment
    • Schmid M., Simpson D., Kalousek F., Gietl C. A cysteine endopeptidase with C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosoma, a putative lytic compartment. Planta. 206:1998;466-475.
    • (1998) Planta , vol.206 , pp. 466-475
    • Schmid, M.1    Simpson, D.2    Kalousek, F.3    Gietl, C.4
  • 36
    • 0029098094 scopus 로고
    • Isolation and characterization of two distinct cDNA clones encoding corn seed cystein proteinases
    • Domoto C., Watanabe H., Abe M., Abe K., Arai S. Isolation and characterization of two distinct cDNA clones encoding corn seed cystein proteinases. Biochim. Biophys. Acta. 1263:1995;241-244.
    • (1995) Biochim. Biophys. Acta , vol.1263 , pp. 241-244
    • Domoto, C.1    Watanabe, H.2    Abe, M.3    Abe, K.4    Arai, S.5
  • 37
    • 0029310645 scopus 로고
    • Molecular cloning and characterization of six cDNAs expressed during glucose starvation in excised maize (Zea mays L.) root tips
    • Chevalier C., Bourgeois E., Pradet A., Raymond P. Molecular cloning and characterization of six cDNAs expressed during glucose starvation in excised maize (Zea mays L.) root tips. Plant Mol. Biol. 28:1995;473-485.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 473-485
    • Chevalier, C.1    Bourgeois, E.2    Pradet, A.3    Raymond, P.4
  • 38
    • 0027690079 scopus 로고
    • Gene expression patterns associated with in vitro tracheary element formation in isolated single mesophyll cells of Zinnia elegans
    • Ye Z. H., Varner J. E. Gene expression patterns associated with in vitro tracheary element formation in isolated single mesophyll cells of Zinnia elegans. Plant Physiol. 103:1993;805-813.
    • (1993) Plant Physiol. , vol.103 , pp. 805-813
    • Ye, Z.H.1    Varner, J.E.2
  • 39
    • 0029310609 scopus 로고
    • Ethylene-regulated expression of a carnation cysteine proteinase during flower petal senescence
    • Jones M. L., Larsen P. B., Woodson W. R. Ethylene-regulated expression of a carnation cysteine proteinase during flower petal senescence. Plant. Mol. Biol. 28:1995;505-512.
    • (1995) Plant. Mol. Biol. , vol.28 , pp. 505-512
    • Jones, M.L.1    Larsen, P.B.2    Woodson, W.R.3
  • 40
    • 0028535314 scopus 로고
    • PCR cloning and expression analysis of cDNAs encoding cysteine proteinases from germinating seeds of Vicia sativa L
    • Becker C., Fischer J., Nong V. H., Munitz K. PCR cloning and expression analysis of cDNAs encoding cysteine proteinases from germinating seeds of Vicia sativa L. Plant Mol. Biol. 26:1994;1207-1212.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1207-1212
    • Becker, C.1    Fischer, J.2    Nong, V.H.3    Munitz, K.4
  • 41
    • 0022828086 scopus 로고
    • Cloning and sequencing of papain-encoding cDNA
    • Cohen L. W., Coghlan V. M., Dihel L. C. Cloning and sequencing of papain-encoding cDNA. Gene. 48:1986;219-227.
    • (1986) Gene , vol.48 , pp. 219-227
    • Cohen, L.W.1    Coghlan, V.M.2    Dihel, L.C.3
  • 43
    • 0025463350 scopus 로고
    • Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted: Sequence and expression of three inducible genes
    • Guerrero F. D., Jones J. T., Mullet J. E. Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted: Sequence and expression of three inducible genes. Plant Mol. Biol. 15:1990;11-26.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 11-26
    • Guerrero, F.D.1    Jones, J.T.2    Mullet, J.E.3
  • 44
    • 0000220251 scopus 로고
    • Cysteine endopeptidase from Vigna mungo: Gene structure and expression
    • Yamuchi D., Akasofu H., Minamikawa T. Cysteine endopeptidase from Vigna mungo: Gene structure and expression. Plant Cell Physiol. 33:1992;789-797.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 789-797
    • Yamuchi, D.1    Akasofu, H.2    Minamikawa, T.3
  • 45
    • 0017846050 scopus 로고
    • The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis
    • Carne A., Moore C. H. The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis. Biochem. J. 173:1978;73-83.
    • (1978) Biochem. J. , vol.173 , pp. 73-83
    • Carne, A.1    Moore, C.H.2
  • 46
    • 0030087809 scopus 로고    scopus 로고
    • Isolation and analysis of cDNAs encoding tomato cysteine proteases expressed during leaf senescence
    • Drake R., John I., Farrell A., Cooper W., Schuch W., Grierson D. Isolation and analysis of cDNAs encoding tomato cysteine proteases expressed during leaf senescence. Plant Mol. Biol. 30:1996;755-767.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 755-767
    • Drake, R.1    John, I.2    Farrell, A.3    Cooper, W.4    Schuch, W.5    Grierson, D.6
  • 47
    • 0026887497 scopus 로고
    • Nucleotide sequence of a gene for an endopeptidase (EP-C1) from Phaseolus vulgaris
    • Ogushi Y., Tanaka T., Yamauchi D., Minamikawa T. Nucleotide sequence of a gene for an endopeptidase (EP-C1) from Phaseolus vulgaris. Plant Mol. Biol. 19:1992;705-706.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 705-706
    • Ogushi, Y.1    Tanaka, T.2    Yamauchi, D.3    Minamikawa, T.4
  • 48
    • 0011742571 scopus 로고
    • Aleurain: A barley thiol protease closely related to mammalian cathepsin H
    • Rogers J. C., Dean D., Heck G. R. Aleurain: A barley thiol protease closely related to mammalian cathepsin H. Proc. Natl. Acad. Sci. USA. 82:1985;6512-6516.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6512-6516
    • Rogers, J.C.1    Dean, D.2    Heck, G.R.3
  • 49
    • 0024066667 scopus 로고
    • The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega
    • Dubois T., Kleinschmidt T., Schnek A. G., Looze Y., Braunitzer G. The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega. Biol. Chem. Hoppe Seyler. 369:1988;741-754.
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 741-754
    • Dubois, T.1    Kleinschmidt, T.2    Schnek, A.G.3    Looze, Y.4    Braunitzer, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.