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Volumn 1804, Issue 9, 2010, Pages 1917-1924

Heterologous expression and purification of a biologically active legume lectin from Cratylia mollis seeds (CRAMOLL 1)

Author keywords

Cratylia mollis seed lectin; Gene synthesis; Heterologous expression; Legume lectins; Protein stability

Indexed keywords

CRAMOLL 1; DNA; LECTIN; MONOSACCHARIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; PLANT LECTIN;

EID: 77955093115     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.06.004     Document Type: Article
Times cited : (19)

References (43)
  • 1
    • 0025222989 scopus 로고
    • Legume lectins-a large family of homologous proteins
    • Sharon N., Lis H. Legume lectins-a large family of homologous proteins. FASEB J. 1990, 4:3198-3208.
    • (1990) FASEB J. , vol.4 , pp. 3198-3208
    • Sharon, N.1    Lis, H.2
  • 2
    • 0029434560 scopus 로고
    • Lectins-proteins with a sweet tooth: functions in cell recognition
    • Sharon N., Lis H. Lectins-proteins with a sweet tooth: functions in cell recognition. Essays Biochem. 1995, 30:59-75.
    • (1995) Essays Biochem. , vol.30 , pp. 59-75
    • Sharon, N.1    Lis, H.2
  • 4
    • 85051589413 scopus 로고
    • Legume storage proteins
    • Marcel Dekker, Inc., New York, J. Kiegeld, G. Galili (Eds.)
    • Vitale A., Bollini R. Legume storage proteins. Seed development and germination 1995, 73-102. Marcel Dekker, Inc., New York. J. Kiegeld, G. Galili (Eds.).
    • (1995) Seed development and germination , pp. 73-102
    • Vitale, A.1    Bollini, R.2
  • 5
    • 0001404121 scopus 로고
    • Synthesis and regulation of major proteins in seeds
    • Higgins T.J.V. Synthesis and regulation of major proteins in seeds. Annu. Rev. Plant Physiol. 1984, 35:191-221.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 191-221
    • Higgins, T.J.V.1
  • 7
    • 0030456404 scopus 로고    scopus 로고
    • Post-translational peptide bond formation during concanavalin A processing in vitro
    • Sheldon P.S., Keen J.N., Bowles D.J. Post-translational peptide bond formation during concanavalin A processing in vitro. Biochem. J. 1996, 320:865-870.
    • (1996) Biochem. J. , vol.320 , pp. 865-870
    • Sheldon, P.S.1    Keen, J.N.2    Bowles, D.J.3
  • 8
    • 0008792588 scopus 로고    scopus 로고
    • Investigation on the origin of the naturally occurring fragments of Cratylia floribunda lectin
    • Grangeiro T.B., Gatehouse J.A., Pereira M.N., Cavada B.S. Investigation on the origin of the naturally occurring fragments of Cratylia floribunda lectin. R. Bras. Fisiol. Veg. 1997, 9:9-13.
    • (1997) R. Bras. Fisiol. Veg. , vol.9 , pp. 9-13
    • Grangeiro, T.B.1    Gatehouse, J.A.2    Pereira, M.N.3    Cavada, B.S.4
  • 10
    • 0026573513 scopus 로고
    • Stability and detection of recombinant pre-pro-concanavalin A after cytoplasmic expression in Escherichia coli
    • Min W., Jones D.H. Stability and detection of recombinant pre-pro-concanavalin A after cytoplasmic expression in Escherichia coli. FEBS Lett. 1992, 301:315-318.
    • (1992) FEBS Lett. , vol.301 , pp. 315-318
    • Min, W.1    Jones, D.H.2
  • 11
    • 33749057675 scopus 로고    scopus 로고
    • Establishment of a heterologous system for the expression of Canavalia brasiliensis lectin: a model for the study of protein splicing
    • Bezerra W.M., Carvalho C.P., Moreira R.A., Grangeiro T.B. Establishment of a heterologous system for the expression of Canavalia brasiliensis lectin: a model for the study of protein splicing. Genet. Mol. Res. 2006, 5:216-223.
    • (2006) Genet. Mol. Res. , vol.5 , pp. 216-223
    • Bezerra, W.M.1    Carvalho, C.P.2    Moreira, R.A.3    Grangeiro, T.B.4
  • 13
    • 0029437098 scopus 로고
    • Purification of a glucose/mannose specific lectin, isoform 1, from seeds of Cratylia mollis Mart. (Camaratu bean)
    • Correia M.T., Coelho L.C. Purification of a glucose/mannose specific lectin, isoform 1, from seeds of Cratylia mollis Mart. (Camaratu bean). Appl. Biochem. Biotechnol. 1995, 55:261-273.
    • (1995) Appl. Biochem. Biotechnol. , vol.55 , pp. 261-273
    • Correia, M.T.1    Coelho, L.C.2
  • 15
    • 0031144784 scopus 로고    scopus 로고
    • Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase
    • Lima V.L.M., Correia M.T.S., Cechinel Y.M.N., Sampaio C.A.M., Owen J.S., Coêlho L.C.B.B. Immobilized Cratylia mollis lectin as a potential matrix to isolate plasma glycoproteins, including lecithin-cholesterol acyltransferase. Carbohydr. Polym. 1997, 33:27-32.
    • (1997) Carbohydr. Polym. , vol.33 , pp. 27-32
    • Lima, V.L.M.1    Correia, M.T.S.2    Cechinel, Y.M.N.3    Sampaio, C.A.M.4    Owen, J.S.5    Coêlho, L.C.B.B.6
  • 16
    • 3042635765 scopus 로고    scopus 로고
    • Ultrastructural analysis and immunocytochemical localization of isolectins in Cratylia mollis seeds
    • Santos A.C., Peixoto C.A., Coelho L.C. Ultrastructural analysis and immunocytochemical localization of isolectins in Cratylia mollis seeds. Micron 2004, 35:613-618.
    • (2004) Micron , vol.35 , pp. 613-618
    • Santos, A.C.1    Peixoto, C.A.2    Coelho, L.C.3
  • 18
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22:1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 19
    • 0141442962 scopus 로고    scopus 로고
    • Overcoming the codon bias of E. coli for enhanced protein expression
    • Novy R., Drott D., Yaeger K., Mierendorf R. Overcoming the codon bias of E. coli for enhanced protein expression. Innovations 2001, 12:1-3.
    • (2001) Innovations , vol.12 , pp. 1-3
    • Novy, R.1    Drott, D.2    Yaeger, K.3    Mierendorf, R.4
  • 20
    • 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
  • 21
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfeld R.A., Lewis U.J., Williams D.E. Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 1962, 195:281-283.
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 22
    • 0000740502 scopus 로고
    • Purification and partial characterization of two lectin isoforms from Cratylia mollis Mart. (Camaratu Bean)
    • Paiva P.M.G., Coelho L.C.B.B. Purification and partial characterization of two lectin isoforms from Cratylia mollis Mart. (Camaratu Bean). Appl. Biochem. Biotechnol. 1992, 36:113-118.
    • (1992) Appl. Biochem. Biotechnol. , vol.36 , pp. 113-118
    • Paiva, P.M.G.1    Coelho, L.C.B.B.2
  • 23
    • 0013801771 scopus 로고
    • Specific binding of concanavalin A to cross-linked dextran gels
    • Agrawal B.B., Goldestein I.J. Specific binding of concanavalin A to cross-linked dextran gels. Biochem. J. 1965, 96:23c-25c.
    • (1965) Biochem. J. , vol.96
    • Agrawal, B.B.1    Goldestein, I.J.2
  • 24
    • 0025101805 scopus 로고
    • Isoelectric focusing studies of concanavalin A and the lentil lectin
    • Bhattacharyya L., Brewer C.F. Isoelectric focusing studies of concanavalin A and the lentil lectin. J. Chromatogr. 1990, 502:131-142.
    • (1990) J. Chromatogr. , vol.502 , pp. 131-142
    • Bhattacharyya, L.1    Brewer, C.F.2
  • 26
    • 0027538064 scopus 로고
    • Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin
    • Schwarz F.P., Puri K.D., Bhat R.G., Surolia A. Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum sativum) lectin, and lentil (Lens culinaris) lectin. J. Biol. Chem. 1993, 268:7668-7677.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7668-7677
    • Schwarz, F.P.1    Puri, K.D.2    Bhat, R.G.3    Surolia, A.4
  • 27
    • 0036747380 scopus 로고    scopus 로고
    • High-pressure as a tool to study some proteins' properties: conformational modification, activity and oligomeric dissociation
    • Lullien-Pellerin V., Balny C. High-pressure as a tool to study some proteins' properties: conformational modification, activity and oligomeric dissociation. Innov. Food Sci. Emerg. 2002, 3:209-221.
    • (2002) Innov. Food Sci. Emerg. , vol.3 , pp. 209-221
    • Lullien-Pellerin, V.1    Balny, C.2
  • 28
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., Royer C.A. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem. Sci. 2001, 26:612-618.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 29
    • 0043018095 scopus 로고    scopus 로고
    • Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease
    • Ferrao-Gonzales A.D., Palmieri L., Valory M., Silva J.L., Lashuel H., Kelly J.W., Foguel D. Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease. J. Mol. Biol. 2003, 328:963-974.
    • (2003) J. Mol. Biol. , vol.328 , pp. 963-974
    • Ferrao-Gonzales, A.D.1    Palmieri, L.2    Valory, M.3    Silva, J.L.4    Lashuel, H.5    Kelly, J.W.6    Foguel, D.7
  • 30
    • 78651030061 scopus 로고
    • Fluorescent indicators of adsorption in aqueous solution and on the solid phase
    • (325th Meeting): xxxi
    • Weber G., Laurence D.J. Fluorescent indicators of adsorption in aqueous solution and on the solid phase. Biochem. J. 1954, 56. (325th Meeting): xxxi.
    • (1954) Biochem. J. , vol.56
    • Weber, G.1    Laurence, D.J.2
  • 31
    • 0000736085 scopus 로고
    • Preparation, crystalline structure and optical properties of the fluorescent probe, 4-4,-bis-1-phenylamino-8-naphthalene sulfonate
    • Farris F.J., Weber G., Paul I.C. Preparation, crystalline structure and optical properties of the fluorescent probe, 4-4,-bis-1-phenylamino-8-naphthalene sulfonate. J. Am. Chem. Soc. 1978, 100:4469-4474.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 4469-4474
    • Farris, F.J.1    Weber, G.2    Paul, I.C.3
  • 33
    • 0038644477 scopus 로고    scopus 로고
    • Denaturant-induced equilibrium unfolding of concanavalin A is expressed by a three-state mechanism and provides an estimate of its protein stability
    • Chatterjee A., Mandal D.K. Denaturant-induced equilibrium unfolding of concanavalin A is expressed by a three-state mechanism and provides an estimate of its protein stability. Biochim. Biophys. Acta 2003, 1648:174-183.
    • (2003) Biochim. Biophys. Acta , vol.1648 , pp. 174-183
    • Chatterjee, A.1    Mandal, D.K.2
  • 34
    • 0021104411 scopus 로고
    • Binding of hydrophobic ligands to plant lectins: titration with arylaminonaphthalenesulfonates
    • Roberts D.D., Goldstein I.J. Binding of hydrophobic ligands to plant lectins: titration with arylaminonaphthalenesulfonates. Arch. Biochem. Biophys. 1983, 224:479-484.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 479-484
    • Roberts, D.D.1    Goldstein, I.J.2
  • 35
    • 0016117743 scopus 로고
    • Agglutination of Trypanosoma cruzi by concanavalin A
    • Alves M.J., Colli W. Agglutination of Trypanosoma cruzi by concanavalin A. J. Protozool. 1974, 21:575-578.
    • (1974) J. Protozool. , vol.21 , pp. 575-578
    • Alves, M.J.1    Colli, W.2
  • 36
    • 0035480468 scopus 로고    scopus 로고
    • A novel model to characterize the electric double layer of lectins from Cratylia mollis (Camaratu bean) and Canavalia ensiformis adsorbed on metallic surface
    • Souza S.R., Correia M.T.S., Pessoa M.M.A., Kennedy J.F., Lima-Filho J.L., Coelho L.C.B.B. A novel model to characterize the electric double layer of lectins from Cratylia mollis (Camaratu bean) and Canavalia ensiformis adsorbed on metallic surface. Carbohydr. Polym. 2001, 46:191-193.
    • (2001) Carbohydr. Polym. , vol.46 , pp. 191-193
    • Souza, S.R.1    Correia, M.T.S.2    Pessoa, M.M.A.3    Kennedy, J.F.4    Lima-Filho, J.L.5    Coelho, L.C.B.B.6
  • 39
    • 47249087220 scopus 로고    scopus 로고
    • Electrochemical evaluation of lectin-sugar interaction on gold electrode modified with colloidal gold and polyvinyl butyral
    • Oliveira M.D.L., Correia M.T.S., Coelho L.C.B.B., Diniz F.B. Electrochemical evaluation of lectin-sugar interaction on gold electrode modified with colloidal gold and polyvinyl butyral. Colloid Surf. B 2008, 66:13-19.
    • (2008) Colloid Surf. B , vol.66 , pp. 13-19
    • Oliveira, M.D.L.1    Correia, M.T.S.2    Coelho, L.C.B.B.3    Diniz, F.B.4
  • 41
    • 45449112140 scopus 로고    scopus 로고
    • Expression of frutalin, an alpha-D-galactose-binding jacalin-related lectin, in the yeast Pichia pastoris
    • Oliveira C., Felix W., Moreira R.A., Teixeira J.A., Domingues L. Expression of frutalin, an alpha-D-galactose-binding jacalin-related lectin, in the yeast Pichia pastoris. Protein Expr. Purif. 2008, 60:188-193.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 188-193
    • Oliveira, C.1    Felix, W.2    Moreira, R.A.3    Teixeira, J.A.4    Domingues, L.5
  • 42
    • 70350567797 scopus 로고    scopus 로고
    • CDNA cloning and functional expression of the alpha-D-galactose-binding lectin frutalin in Escherichia coli
    • Oliveira C., Costa S., Teixeira J.A., Domingues L. cDNA cloning and functional expression of the alpha-D-galactose-binding lectin frutalin in Escherichia coli. Mol. Biotechnol. 2009, 43:212-220.
    • (2009) Mol. Biotechnol. , vol.43 , pp. 212-220
    • Oliveira, C.1    Costa, S.2    Teixeira, J.A.3    Domingues, L.4
  • 43
    • 0015935084 scopus 로고
    • The binding properties of dimeric and tetrameric concanavalin A. Binding of ligands to noninteracting macromolecular acceptors
    • McKenzie G.H., Sawyer W.H. The binding properties of dimeric and tetrameric concanavalin A. Binding of ligands to noninteracting macromolecular acceptors. J. Biol. Chem. 1973, 248:549-556.
    • (1973) J. Biol. Chem. , vol.248 , pp. 549-556
    • McKenzie, G.H.1    Sawyer, W.H.2


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