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Volumn 19, Issue 1, 2000, Pages 39-49

Isolation and characterization of a cysteine protease from the latex of araujia hortorum fruits

Author keywords

Araujia hortorum; Asciepiadaceae; Latex; Milkweed; Plant proteases

Indexed keywords

ALANINE; ARAUJIAIN H 1; ASPARAGINE; CASEIN; CYSTEINE PROTEINASE; GLUTAMINE DERIVATIVE; GLYCINE; LATEX; LEUCINE; MERCURIC CHLORIDE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 52849101977     PISSN: 15723887     EISSN: 15734943     Source Type: Journal    
DOI: 10.1023/A:1007042825783     Document Type: Article
Times cited : (63)

References (57)
  • 1
    • 0018786627 scopus 로고
    • Studies on proteinases from Calotropis gigantea latex. I. Purification and some properties of two proteinases containing carbohydrate
    • Abraham, K. I., and Joshi, P. N. (1979a). Studies on proteinases from Calotropis gigantea latex. I. Purification and some properties of two proteinases containing carbohydrate, Biochim. Biophys. Acta 568, 111-119.
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 111-119
    • Abraham, K.I.1    Joshi, P.N.2
  • 2
    • 0018786621 scopus 로고
    • Studies on proteinases from Calotropis gigantea latex. II. Physico-chemical properties of calotropain-FI and F-II
    • Abraham, K. I., and Joshi, P. N. (1979e). Studies on proteinases from Calotropis gigantea latex. II. Physico-chemical properties of calotropain-FI and F-II, Biochim. Biophys. Acta 568, 120-126.
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 120-126
    • Abraham, K.I.1    Joshi, P.N.2
  • 4
    • 0031742430 scopus 로고    scopus 로고
    • Comparison of Asclepiadaceae latex proteases and characterization of Morrenia brachystephana Griseb. cysteine peptidases
    • Arribére, M. C., Cortadi, A. A., Gattuso, M. A., Bettiol, M. P., Priolo, N. S., and Caffini, N. O. (1998). Comparison of Asclepiadaceae latex proteases and characterization of Morrenia brachystephana Griseb. cysteine peptidases, Phytochem. Anal. 9, 1-7.
    • (1998) Phytochem. Anal. , vol.9 , pp. 1-7
    • Arribére, M.C.1    Cortadi, A.A.2    Gattuso, M.A.3    Bettiol, M.P.4    Priolo, N.S.5    Caffini, N.O.6
  • 7
    • 0019948262 scopus 로고
    • L-transEpoxysuccinyl-leucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A. J., Kembhavi, A. A., Brown, M. A., Kirschke, H., Knight, C.G., Tamai, M., and Hanada, K. (1982). L-transEpoxysuccinyl-leucylamido (4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L, Biochem. J. 201, 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 9
    • 0030931105 scopus 로고    scopus 로고
    • Proteinase A, a storageglobulin-degrading endopeptidase of vetch (Vicia saliva L.) seeds, is not involved in early steps of storage-protein mobilization
    • Becker, C., Senyuk, V. I., Shutov, A. D., Nong, V. H., Fischer, J., Horstmann, C., and Muntz, K. (1997). Proteinase A, a storageglobulin-degrading endopeptidase of vetch (Vicia saliva L.) seeds, is not involved in early steps of storage-protein mobilization, Ear. J. Biochem. 248, 304-312.
    • (1997) Ear. J. Biochem. , vol.248 , pp. 304-312
    • Becker, C.1    Senyuk, V.I.2    Shutov, A.D.3    Nong, V.H.4    Fischer, J.5    Horstmann, C.6    Muntz, K.7
  • 10
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interactions of plants with other organisms
    • Dalling, M. J., ed., CRC Press, Boca Raton, Florida
    • Boiler, T. (1986). Roles of proteolytic enzymes in interactions of plants with other organisms, in Plant Proteolytic Enzymes (Dalling, M. J., ed.), CRC Press, Boca Raton, Florida, Vol. I, pp. 76-86.
    • (1986) Plant Proteolytic Enzymes , vol.1 , pp. 76-86
    • Boiler, T.1
  • 11
    • 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. M. (1976). A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0018799155 scopus 로고
    • Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. (milkweed)
    • Brockbank, W. J., and Lynn, K. R. (1979). Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. (milkweed), Biochim. Biophys. Acta 578, 113-122.
    • (1979) Biochim. Biophys. Acta , vol.578 , pp. 113-122
    • Brockbank, W.J.1    Lynn, K.R.2
  • 14
    • 0003371076 scopus 로고
    • The isoelectric point of asclepain
    • Carpenter, D. C., and Lovelace, F. E. (1943). The isoelectric point of asclepain, J. Am. Chem. Soc. 65, 2364-2365.
    • (1943) J. Am. Chem. Soc. , vol.65 , pp. 2364-2365
    • Carpenter, D.C.1    Lovelace, F.E.2
  • 15
    • 0033117455 scopus 로고    scopus 로고
    • Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea
    • Cercos, M., Santamaria, S., and Carbonell, J. (1999). Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea, Plant Physiol. 119, 1341-1348.
    • (1999) Plant Physiol. , vol.119 , pp. 1341-1348
    • Cercos, M.1    Santamaria, S.2    Carbonell, J.3
  • 16
    • 0028431691 scopus 로고
    • Ethylene regulates the expression of a cysteine proteinase gene during germination of chickpea (Cicer arietinum L.)
    • Cervantes, E., Rodriguez, A., and Nicolas, G. (1994). Ethylene regulates the expression of a cysteine proteinase gene during germination of chickpea (Cicer arietinum L.), Plant Mol. Biol. 25, 207-215.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 207-215
    • Cervantes, E.1    Rodriguez, A.2    Nicolas, G.3
  • 17
    • 0033533253 scopus 로고    scopus 로고
    • The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome
    • Choi, K. H., Laursen, R. A., and Allen, K. N. (1999). The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale, Biochemistry 38, 11624-11633.
    • (1999) Zingiber Officinale, Biochemistry , vol.38 , pp. 11624-11633
    • Choi, K.H.1    Laursen, R.A.2    Allen, K.N.3
  • 18
    • 0024301797 scopus 로고
    • Spatial patterns of gene expression in Brassica napus seedlings: Identification of a cortex-specific gene and localization of mRNAs encoding isocitrate lyase and a polypeptide homologous to proteinases
    • Dietrich, R. A., Maslyar, D. J., Heupel, R. C., and Harada, J. J. (1989). Spatial patterns of gene expression in Brassica napus seedlings: Identification of a cortex-specific gene and localization of mRNAs encoding isocitrate lyase and a polypeptide homologous to proteinases, Plant Cell 1, 73-80.
    • (1989) Plant Cell , vol.1 , pp. 73-80
    • Dietrich, R.A.1    Maslyar, D.J.2    Heupel, R.C.3    Harada, J.J.4
  • 20
    • 0004262303 scopus 로고
    • Academic Press, New York
    • Dixon, M., and Webb, E. C. (1979). Enzymes, Academic Press, New York, pp. 164-169.
    • (1979) Enzymes , pp. 164-169
    • Dixon, M.1    Webb, E.C.2
  • 21
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F. (1956). Colorimetric method for determination of sugars and related substances, Anal. Chem. 28, 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 22
    • 0029549481 scopus 로고
    • Inhibition of leaf senescence by autoregulated production of cytokinin
    • Gan, S., and Amasino, R. M. (1995). Inhibition of leaf senescence by autoregulated production of cytokinin, Science 270, 1986-1988.
    • (1995) Science , vol.270 , pp. 1986-1988
    • Gan, S.1    Amasino, R.M.2
  • 23
    • 0028061439 scopus 로고
    • Differential gene expression in an actinorhizal symbiosis: Evidence for a nodulespecific cysteine proteinase
    • Goetting-Minesky, P., and Mullin, B. C. (1994). Differential gene expression in an actinorhizal symbiosis: Evidence for a nodulespecific cysteine proteinase, Proc. Natl. Acad. Sci. USA 91, 9891-9895.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9891-9895
    • Goetting-Minesky, P.1    Mullin, B.C.2
  • 25
    • 0003311632 scopus 로고
    • Plant proteases. II. pH-activity curves
    • Greenberg, D.M., and Winnick, T. (1940). Plant proteases. II. pH-activity curves, J. Biol. Chem. 135, 775-780.
    • (1940) J. Biol. Chem. , vol.135 , pp. 775-780
    • Greenberg, D.M.1    Winnick, T.2
  • 26
    • 0031745660 scopus 로고    scopus 로고
    • Isolation and characterization of two forms of an acidic bromelain stem proteinase
    • Harrach, T., Eckert, K., Maurer, H. R., Machleidt, I., Machleidt, W., and Nuck, R. (1998). Isolation and characterization of two forms of an acidic bromelain stem proteinase, J. Protein Chem. 17, 351-361.
    • (1998) J. Protein Chem. , vol.17 , pp. 351-361
    • Harrach, T.1    Eckert, K.2    Maurer, H.R.3    Machleidt, I.4    Machleidt, W.5    Nuck, R.6
  • 27
    • 0028446499 scopus 로고
    • Primary structure of CC-III, the glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook
    • Jaziri, M., Kleinschmidt, T., Walraevens, V., Schnek, A. G., and Looze, Y. (1994). Primary structure of CC-III, the glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook, Biol. Chem. Hoppe-Seyler 375, 379-385.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 379-385
    • Jaziri, M.1    Kleinschmidt, T.2    Walraevens, V.3    Schnek, A.G.4    Looze, Y.5
  • 28
    • 0026625627 scopus 로고
    • A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation
    • Kalinski, A., Melroy, D. L., Dwivedi, R. S., and Herman, E. M. (1992). A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation, J. Biol. Chem. 267, 12068-12076.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12068-12076
    • Kalinski, A.1    Melroy, D.L.2    Dwivedi, R.S.3    Herman, E.M.4
  • 29
    • 0030298354 scopus 로고    scopus 로고
    • Expression of cysteine protease genes in pea nodule development and senescence
    • Kardailsky, I. V., and Brewin, N. J. (1996). Expression of cysteine protease genes in pea nodule development and senescence, Mol. Plant Microbe Interact. 9, 689-695.
    • (1996) Mol. Plant Microbe Interact. , vol.9 , pp. 689-695
    • Kardailsky, I.V.1    Brewin, N.J.2
  • 30
    • 0027274695 scopus 로고
    • Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana
    • Koizumi, M., Yamaguchi-Shinozaki, K., Tsuji, H., and Shinozaki, K. (1993). Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana. Gene 129, 175-182.
    • (1993) Gene , vol.129 , pp. 175-182
    • Koizumi, M.1    Yamaguchi-Shinozaki, K.2    Tsuji, H.3    Shinozaki, K.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0028526562 scopus 로고
    • Enzymatic production of protein hydrolyzates for food use
    • Lahl, W. J., and Brown, S. D. (1994). Enzymatic production of protein hydrolyzates for food use, Food Technol. 48, 68-71.
    • (1994) Food Technol. , vol.48 , pp. 68-71
    • Lahl, W.J.1    Brown, S.D.2
  • 34
    • 0019324038 scopus 로고
    • Multiple forms of the asclepains, cysteinyl proteases from milkweed
    • Lynn, K. R., Brockbank, W. J., and Clevette-Radford, N. A. (1980a). Multiple forms of the asclepains, cysteinyl proteases from milkweed, Biochim. Biophys. Acta 612, 119-125.
    • (1980) Biochim. Biophys. Acta , vol.612 , pp. 119-125
    • Lynn, K.R.1    Brockbank, W.J.2    Clevette-Radford, N.A.3
  • 35
    • 0019330413 scopus 로고
    • Homologies of the N-terminal sequences of asclepains and papain
    • Lynn, K. R., Yaguchi, M., and Roy, C. (1980e). Homologies of the N-terminal sequences of asclepains and papain, Biochim. Biophys. Acta 624, 579-580.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 579-580
    • Lynn, K.R.1    Yaguchi, M.2    Roy, C.3
  • 36
    • 0028526893 scopus 로고
    • Physicochemical and functional properties of protein hydrolysates in nutritional products
    • Mahmoud, M. I. (1994). Physicochemical and functional properties of protein hydrolysates in nutritional products, Food Technol. 48, 89-95.
    • (1994) Food Technol. , vol.48 , pp. 89-95
    • Mahmoud, M.I.1
  • 37
    • 0019041178 scopus 로고
    • Isolation, crystallization, and properties of calotropins DI and DH from Calotropis gigantea
    • Pal, G., and Sinha, N. K. (1980). Isolation, crystallization, and properties of calotropins DI and DH from Calotropis gigantea. Arch. Biochem. Biophys. 202, 321-329.
    • (1980) Arch. Biochem. Biophys. , vol.202 , pp. 321-329
    • Pal, G.1    Sinha, N.K.2
  • 38
    • 0033136476 scopus 로고    scopus 로고
    • Characterization of three distinct cDNA clones encoding cysteine proteinases from maize (Zea mays L.) callus
    • Pechan, T., Jiang, B., Sleekier, D., Ye, L., Lin, L., Luthe, D. S., and Williams, W. P. (1999). Characterization of three distinct cDNA clones encoding cysteine proteinases from maize (Zea mays L.) callus, Plant Mol. Biol. 40, 111-119.
    • (1999) Plant Mol. Biol. , vol.40 , pp. 111-119
    • Pechan, T.1    Jiang, B.2    Sleekier, D.3    Ye, L.4    Lin, L.5    Luthe, D.S.6    Williams, W.P.7
  • 39
    • 0024978614 scopus 로고
    • Nucleotide sequence of actinidin, a kiwi fruit protease
    • Podivinsky, E., Forster, R. L., and Gardner, R. C. (1989). Nucleotide sequence of actinidin, a kiwi fruit protease, Nucleic Acids Res. 17, 8363.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8363
    • Podivinsky, E.1    Forster, R.L.2    Gardner, R.C.3
  • 40
    • 0000875075 scopus 로고
    • Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinensis
    • Praekelt, U.M., McKee, R. A., and Smith, H. (1988). Molecular analysis of actinidin, the cysteine proteinase of Actinidia chinensis. Plant Mol. Biol. 10, 193-202.
    • (1988) Plant Mol. Biol. , vol.10 , pp. 193-202
    • Praekelt, U.M.1    McKee, R.A.2    Smith, H.3
  • 43
    • 0030918758 scopus 로고    scopus 로고
    • Proteinase A-like enzyme from germinated kidney bean seeds. Its action on phaseolin and vicilin
    • Rotari, V., Senyuk, V., Horstmann, C., Jivotovskaya, A., and Vaintraub, I. (1997). Proteinase A-like enzyme from germinated kidney bean seeds. Its action on phaseolin and vicilin, Physiol. Plantarum 100, 171-177.
    • (1997) Physiol. Plantarum , vol.100 , pp. 171-177
    • Rotari, V.1    Senyuk, V.2    Horstmann, C.3    Jivotovskaya, A.4    Vaintraub, I.5
  • 45
    • 0021457126 scopus 로고
    • Comparative studies on calotropins DI and DII from the latex of Calotropis gigantea
    • Sengupta, A., Bhattacharya, D., Pal, G., and Sinha, N. K. (1984). Comparative studies on calotropins DI and DII from the latex of Calotropis gigantea, Arch. Biochem. Biophys. 232, 17-25.
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 17-25
    • Sengupta, A.1    Bhattacharya, D.2    Pal, G.3    Sinha, N.K.4
  • 46
    • 0016334079 scopus 로고
    • α-CBZ-L-lysine p-nitrophenyl ester and N-CBZ-glycine p-nitrophenyl ester as substrates
    • α-CBZ-L-lysine p-nitrophenyl ester and N-CBZ-glycine p-nitrophenyl ester as substrates, Analyt. Biochem. 62, 478-4184.
    • (1974) Analyt. Biochem. , vol.62 , pp. 478-4184
    • Silverstein, R.M.1
  • 47
    • 0007231824 scopus 로고    scopus 로고
    • Nucleotide sequence of a cDNA (Accession No. U52970) encoding a Cys proteinase from germinating bean cotyledons (PGR97-055)
    • Sohlberg, L., and Sussex, I. M. (1997). Nucleotide sequence of a cDNA (Accession No. U52970) encoding a Cys proteinase from germinating bean cotyledons (PGR97-055), Plant Physiol. 113, 1463.
    • (1997) Plant Physiol. , vol.113 , pp. 1463
    • Sohlberg, L.1    Sussex, I.M.2
  • 48
    • 0025984862 scopus 로고
    • Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid
    • Sprensen, S. B., Sprensen, T. L., and Breddam, K. (1991). Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid, FEBS Lett. 294, 195-197.
    • (1991) FEBS Lett. , vol.294 , pp. 195-197
    • Sprensen, S.B.1    Sprensen, T.L.2    Breddam, K.3
  • 50
    • 0029310458 scopus 로고
    • Up-regulation of a cysteine protease accompanies the ethyleneinsensitive senescence of daylily (Hemerocallis) flowers
    • Valpuesta, V., Lange, N. E., Guerrero, C., and Reid, M. S (1995). Up-regulation of a cysteine protease accompanies the ethyleneinsensitive senescence of daylily (Hemerocallis) flowers, Plant Mol. Biol. 28, 575-582.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 575-582
    • Valpuesta, V.1    Lange, N.E.2    Guerrero, C.3    Reid, M.S.4
  • 51
    • 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., and Aral, S. (1991). Molecular cloning and gibberellin-induced expression of multiple cysteine proteinases of rice seeds (oryzains), J. Biol. Chem. 266, 16897-16902.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16897-16902
    • Watanabe, H.1    Abe, K.2    Emori, Y.3    Hosoyama, H.4    Aral, S.5
  • 52
    • 0025008745 scopus 로고
    • The amino acid sequence of chymopapain from Carica papaya
    • Watson, D. C., Yaguchi, M., and Lynn. K. R. (1990). The amino acid sequence of chymopapain from Carica papaya, Biochem. J. 266, 75-81.
    • (1990) Biochem. J. , vol.266 , pp. 75-81
    • Watson, D.C.1    Yaguchi, M.2    Lynn, K.R.3
  • 55
    • 0002825020 scopus 로고
    • Physicochemical properties of the proteolytic enzyme from the latex of the milkweed, Asclepias speciosa Tort. Some comparisons with other proteases
    • Winnick, T., Davis, A. R., and Greenberg, D. M. (1940). Physicochemical properties of the proteolytic enzyme from the latex of the milkweed, Asclepias speciosa Tort. Some comparisons with other proteases, J. Gen. Physiol. 23, 275-288.
    • (1940) J. Gen. Physiol. , vol.23 , pp. 275-288
    • Winnick, T.1    Davis, A.R.2    Greenberg, D.M.3
  • 56
    • 0000220251 scopus 로고
    • Cysteine endopeptidase from Vigna mungo. Gene structure and expression
    • Yamauchi, D., Akasofu, H., and Minamikawa, T. (1992). Cysteine endopeptidase from Vigna mungo. Gene structure and expression, Plant Cell Physiol. 33, 789-797.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 789-797
    • Yamauchi, D.1    Akasofu, H.2    Minamikawa, T.3
  • 57
    • 0027690079 scopus 로고
    • Gene expression patterns associated with in vitro tracheary element formation in isolated single mesophyll cells of Zinnia elegans
    • Ye, Z. H., and Varner, J. E. (1993). Gene expression patterns associated with in vitro tracheary element formation in isolated single mesophyll cells of Zinnia elegans. Plant Physiol. 103, 805-813.
    • (1993) Plant Physiol. , vol.103 , pp. 805-813
    • Ye, Z.H.1    Varner, J.E.2


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