메뉴 건너뛰기




Volumn 49, Issue 7, 2011, Pages 721-728

Biochemical and spectroscopic characterization of a novel metalloprotease, cotinifolin from an antiviral plant shrub: Euphorbia cotinifolia

Author keywords

Caribbean copper plant; Cotinifolin; Euphorbia cotinifolia; Euphorbiaceae; Metalloprotease

Indexed keywords

DETERGENT; DIVALENT CATION; METALLOPROTEINASE; VEGETABLE PROTEIN;

EID: 79956291544     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2011.03.016     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 24344495312 scopus 로고    scopus 로고
    • Plant serine proteases: biochemical, physiological and molecular features
    • Antao C.M., Malcata F.X. Plant serine proteases: biochemical, physiological and molecular features. Plant Physiol. Biochem. 2005, 43:637-650.
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 637-650
    • Antao, C.M.1    Malcata, F.X.2
  • 2
    • 48049104106 scopus 로고    scopus 로고
    • Indicain, a dimeric serine protease from Morus indica cv. K2
    • Singh V.K., Patel A.K., Moir A.J., Jagannadham M.V. Indicain, a dimeric serine protease from Morus indica cv. K2. Phytochemistry 2008, 69:2110-2119.
    • (2008) Phytochemistry , vol.69 , pp. 2110-2119
    • Singh, V.K.1    Patel, A.K.2    Moir, A.J.3    Jagannadham, M.V.4
  • 3
    • 0343994324 scopus 로고
    • Enzymes extracellular
    • Academic Press
    • Priest F.G. Enzymes extracellular. Encyclopedia of Microbiology 1992, vol. 2:451-460. Academic Press.
    • (1992) Encyclopedia of Microbiology , vol.2 , pp. 451-460
    • Priest, F.G.1
  • 4
    • 0011873937 scopus 로고
    • Microbial proteases
    • Keay L. Microbial proteases. Process Biochem. 1971, 6:17-21.
    • (1971) Process Biochem. , vol.6 , pp. 17-21
    • Keay, L.1
  • 5
    • 0009817773 scopus 로고
    • Proteinases
    • Academic Press, New York, A.H. Rose (Ed.)
    • Aunstrup K. Proteinases. Microbial Enzymes and Bioconversions 1980, 49-144. Academic Press, New York. A.H. Rose (Ed.).
    • (1980) Microbial Enzymes and Bioconversions , pp. 49-144
    • Aunstrup, K.1
  • 7
    • 0026440343 scopus 로고
    • Mitochondrial processing proteinase - a general processing proteinase of spinach leaf mitochondria is a membrane-bound enzyme
    • Eriksson A.C., Glaser E. Mitochondrial processing proteinase - a general processing proteinase of spinach leaf mitochondria is a membrane-bound enzyme. Biochim. Biophys. Acta 1992, 1140:208-214.
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 208-214
    • Eriksson, A.C.1    Glaser, E.2
  • 8
    • 79956335519 scopus 로고
    • Characterization of the soluble proteolytic enzymes of green malt, in: Proceedings of the 13th European Brewery Convention Congress, Madrid
    • T.M. Enari, J. Mikola, Characterization of the soluble proteolytic enzymes of green malt, in: Proceedings of the 13th European Brewery Convention Congress, Madrid, 1967, pp. 9-16.
    • (1967) , pp. 9-16
    • Enari, T.M.1    Mikola, J.2
  • 9
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 p.otein
    • Lindahl M., Spetea C., Hundal T., Oppenheim A.B., Adam Z., Andersson B. The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 p.otein. Plant Cell 2000, 12:419-431.
    • (2000) Plant Cell , vol.12 , pp. 419-431
    • Lindahl, M.1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 10
    • 0030471302 scopus 로고    scopus 로고
    • Protein stability and degradation in chloroplasts
    • Adam Z. Protein stability and degradation in chloroplasts. Plant Mol. Biol. 1996, 32:773-783.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 773-783
    • Adam, Z.1
  • 11
    • 0032560485 scopus 로고    scopus 로고
    • A chloroplast processing enzyme functions as the general stromal processing peptidase
    • Richter S., Lamppa G.K. A chloroplast processing enzyme functions as the general stromal processing peptidase. Proc. Natl. Acad. Sci. 1998, 95:7463-7468.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 7463-7468
    • Richter, S.1    Lamppa, G.K.2
  • 12
    • 0000245936 scopus 로고
    • Purification and developmental analysis of a metalloendoproteinase from the leaves of glycine max
    • Graham J.S., Xiong J., Gillikin J.W. Purification and developmental analysis of a metalloendoproteinase from the leaves of glycine max. Plant Physiol. 1991, 97:786-792.
    • (1991) Plant Physiol. , vol.97 , pp. 786-792
    • Graham, J.S.1    Xiong, J.2    Gillikin, J.W.3
  • 13
    • 4444375447 scopus 로고    scopus 로고
    • Characterization of senescence-associated proteases in postharvest broccoli florets
    • Wang Y.T., Yang C.Y., Chen Y.T., Lin Y., Shaw J.F. Characterization of senescence-associated proteases in postharvest broccoli florets. Plant Physiol. Biochem. 2004, 42:663-670.
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 663-670
    • Wang, Y.T.1    Yang, C.Y.2    Chen, Y.T.3    Lin, Y.4    Shaw, J.F.5
  • 14
    • 0035739096 scopus 로고    scopus 로고
    • Identification of metalloprotease gene families in sugarcane
    • Ramos O.H.P., Selistre-de-Araujo H.S. Identification of metalloprotease gene families in sugarcane. Genet. Mol.Bio 2001, 24:285-290.
    • (2001) Genet. Mol.Bio , vol.24 , pp. 285-290
    • Ramos, O.H.P.1    Selistre-de-Araujo, H.S.2
  • 16
    • 0015766533 scopus 로고
    • Purification and properties of neutral proteinase I, from Aspergillus oryzae
    • Nakadai T., Nasumo S., Iguchi N. Purification and properties of neutral proteinase I, from Aspergillus oryzae. Agric. Biol. Chem. 1973, 37:2695-2701.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 2695-2701
    • Nakadai, T.1    Nasumo, S.2    Iguchi, N.3
  • 19
    • 0034955223 scopus 로고    scopus 로고
    • Purification and characterization of a 43.5 kDa keratinolytic metalloprotease from Microsporum canis
    • Brouta F., Descamps F., Fett T., Losson B., Gerday C., Mignon B. Purification and characterization of a 43.5 kDa keratinolytic metalloprotease from Microsporum canis. Med. Mycol. 2001, 39:269-275.
    • (2001) Med. Mycol. , vol.39 , pp. 269-275
    • Brouta, F.1    Descamps, F.2    Fett, T.3    Losson, B.4    Gerday, C.5    Mignon, B.6
  • 20
    • 27944465216 scopus 로고    scopus 로고
    • Purification and some properties of a metalloprotease from sorghum malt variety KSV8-1
    • Ogbonna A.C., Okolo B.N. Purification and some properties of a metalloprotease from sorghum malt variety KSV8-1. World J. Microbio. Biotech. 2005, 21:1051-1056.
    • (2005) World J. Microbio. Biotech. , vol.21 , pp. 1051-1056
    • Ogbonna, A.C.1    Okolo, B.N.2
  • 21
    • 75349099771 scopus 로고    scopus 로고
    • Purification and properties of cold-active metalloprotease from Curtobacterium luteum and effect of culture conditions on production
    • Kuddus M., Ramteke P.W. Purification and properties of cold-active metalloprotease from Curtobacterium luteum and effect of culture conditions on production. Chin. J. Biotechnol. 2009, 24:2074-2080.
    • (2009) Chin. J. Biotechnol. , vol.24 , pp. 2074-2080
    • Kuddus, M.1    Ramteke, P.W.2
  • 22
    • 0004054634 scopus 로고    scopus 로고
    • Protein and enzyme techniques
    • Cambridge University Press, K. Wilson, J. Walker (Eds.)
    • Wilson K. Protein and enzyme techniques. Practical Biochemistry, Principles and Techniques 1996, pp.162-226. Cambridge University Press. K. Wilson, J. Walker (Eds.).
    • (1996) Practical Biochemistry, Principles and Techniques
    • Wilson, K.1
  • 23
    • 0014878487 scopus 로고
    • Acid protease from germinated sorghum.1. Purification and characterization of enzyme
    • Garg G.K., Virupaks T.K. Acid protease from germinated sorghum.1. Purification and characterization of enzyme. Eur. J. Biochem. 1970, 17:4-12.
    • (1970) Eur. J. Biochem. , vol.17 , pp. 4-12
    • Garg, G.K.1    Virupaks, T.K.2
  • 24
    • 27944448211 scopus 로고
    • Protein inhibitors of proteinases
    • North-Holland Pub, Amsterdam, A.J. Barrett (Ed.)
    • Barrett A.J. Protein inhibitors of proteinases. Proteinases in Mammalian Cells and Tissues 1977, 113-118. North-Holland Pub, Amsterdam. A.J. Barrett (Ed.).
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 113-118
    • Barrett, A.J.1
  • 25
    • 0002931459 scopus 로고
    • Purification and partial characterization of a dipeptidase from barley
    • Sopanen T. Purification and partial characterization of a dipeptidase from barley. Plant Physiol. 1976, 57:867-871.
    • (1976) Plant Physiol. , vol.57 , pp. 867-871
    • Sopanen, T.1
  • 26
    • 3242783506 scopus 로고    scopus 로고
    • Purification and characterization of two distinct metalloproteases secreted by the entomopathogenic bacterium Photorhabdus sp strain Az29
    • Cabral C.M., Cherqui A., Pereira A., Simoes N. Purification and characterization of two distinct metalloproteases secreted by the entomopathogenic bacterium Photorhabdus sp strain Az29. App. Env. Microbio. 2004, 70:3831-3838.
    • (2004) App. Env. Microbio. , vol.70 , pp. 3831-3838
    • Cabral, C.M.1    Cherqui, A.2    Pereira, A.3    Simoes, N.4
  • 28
    • 40549120904 scopus 로고    scopus 로고
    • A stable serine protease, wrightin, from the latex of the plant Wrightia tinctoria (Roxb.) R. Br.: purification and biochemical properties
    • Tomar R., Kumar R., Jagannadham M.V. A stable serine protease, wrightin, from the latex of the plant Wrightia tinctoria (Roxb.) R. Br.: purification and biochemical properties. J Agric. Food Chem. 2008, 56:1479-1487.
    • (2008) J Agric. Food Chem. , vol.56 , pp. 1479-1487
    • Tomar, R.1    Kumar, R.2    Jagannadham, M.V.3
  • 29
    • 70449678591 scopus 로고    scopus 로고
    • Crinumin, a chymotrypsin-like but glycosylated serine protease from Crinum asiaticum: purification and physicochemical characterisation
    • Singh K.A., Kumar R., Rao G.R.K., Jagannadham M.V. Crinumin, a chymotrypsin-like but glycosylated serine protease from Crinum asiaticum: purification and physicochemical characterisation. Food Chem. 2010, 119:1352-1358.
    • (2010) Food Chem. , vol.119 , pp. 1352-1358
    • Singh, K.A.1    Kumar, R.2    Rao, G.R.K.3    Jagannadham, M.V.4
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0033550064 scopus 로고    scopus 로고
    • 8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions
    • Ali V., Prakash K., Kulkarni S., Ahmad A., Madhusudan K.P., Bhakuni V. 8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions. Biochemistry 1999, 38:13635-13642.
    • (1999) Biochemistry , vol.38 , pp. 13635-13642
    • Ali, V.1    Prakash, K.2    Kulkarni, S.3    Ahmad, A.4    Madhusudan, K.P.5    Bhakuni, V.6
  • 34
    • 0012387041 scopus 로고    scopus 로고
    • Chemical methods of analysis of glycoprotein
    • Humana Press, Totowa, NJ, J.M. Walker (Ed.)
    • Hounsell E.F., Davies M.J., Smith K.D. Chemical methods of analysis of glycoprotein. The Protein Protocols Handbook 1997, 633-634. Humana Press, Totowa, NJ. J.M. Walker (Ed.).
    • (1997) The Protein Protocols Handbook , pp. 633-634
    • Hounsell, E.F.1    Davies, M.J.2    Smith, K.D.3
  • 36
    • 0001340623 scopus 로고
    • Enzymes
    • Wiley and Sons, New York
    • Segel I.H. Enzymes. Biochemical Calculation 1976, 208-323. Wiley and Sons, New York. second ed.
    • (1976) Biochemical Calculation , pp. 208-323
    • Segel, I.H.1
  • 37
    • 0000154726 scopus 로고
    • Immunodiffusion and immunoelectrophoresis
    • Blackwell, Oxford, U.K, D.M. Weir, L.A. Herzerberg, C. Blackwell, L.A. Herzerberg (Eds.)
    • Ouchterlony O., Nilsson L.A. Immunodiffusion and immunoelectrophoresis. Handbook of Experimental Immunology 1986, vol. 1:32.31-32.50. Blackwell, Oxford, U.K. D.M. Weir, L.A. Herzerberg, C. Blackwell, L.A. Herzerberg (Eds.).
    • (1986) Handbook of Experimental Immunology , vol.1
    • Ouchterlony, O.1    Nilsson, L.A.2
  • 38
    • 0018396426 scopus 로고
    • Purification and characterization of a Serratia marcescens metalloprotease
    • Lyerly D., Kreger A. Purification and characterization of a Serratia marcescens metalloprotease. Infect. Immun. 1979, 24:411-421.
    • (1979) Infect. Immun. , vol.24 , pp. 411-421
    • Lyerly, D.1    Kreger, A.2
  • 39
    • 0025645610 scopus 로고
    • Purification and characterization of acidolysin, an acidic metalloprotease produced by clostridium-acetobutylicum Atcc-824
    • Croux C., Paquet V., Goma G., Soucaille P. Purification and characterization of acidolysin, an acidic metalloprotease produced by clostridium-acetobutylicum Atcc-824. App. Env. Microbio. 1990, 56:3634-3642.
    • (1990) App. Env. Microbio. , vol.56 , pp. 3634-3642
    • Croux, C.1    Paquet, V.2    Goma, G.3    Soucaille, P.4
  • 40
    • 0027755968 scopus 로고
    • Purification and characterization of a thermostable neutral metalloprotease I from Chloroflexus aurantiacus J-10-fl
    • Watanabe A., Kamio Y., Kimura W., Izaki K. Purification and characterization of a thermostable neutral metalloprotease I from Chloroflexus aurantiacus J-10-fl. Biosci. Biotech. Biochem. 1993, 57:2160-2165.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 2160-2165
    • Watanabe, A.1    Kamio, Y.2    Kimura, W.3    Izaki, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.