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Volumn 67, Issue 2, 2009, Pages 82-87

Refolding and purification of the human secreted group IID phospholipase A2 expressed as inclusion bodies in Escherichia coli

Author keywords

hsPLA2 IID; Inclusion body; Phospholipid hydrolysis; Refolding

Indexed keywords

GUANIDINE; PHOSPHOLIPASE A2; PHOSPHOLIPID; RECOMBINANT PROTEIN;

EID: 67650140709     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.04.006     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0023034069 scopus 로고
    • Role of secretory phospholipases A2 in the pathobiology of disease
    • Vadas P., and Pruzanski W. Role of secretory phospholipases A2 in the pathobiology of disease. Lab. Invest. 55 (1986) 391-404
    • (1986) Lab. Invest. , vol.55 , pp. 391-404
    • Vadas, P.1    Pruzanski, W.2
  • 2
    • 0024827770 scopus 로고
    • Thromboxane A2: its generation and role in platelet activation
    • Arita H., Nakano T., and Hanasaki K. Thromboxane A2: its generation and role in platelet activation. Prog. Lipid Res. 28 (1989) 273-301
    • (1989) Prog. Lipid Res. , vol.28 , pp. 273-301
    • Arita, H.1    Nakano, T.2    Hanasaki, K.3
  • 3
    • 0028338536 scopus 로고
    • Diversity of group types, regulation, and function of phospholipase A2
    • Dennis E.A. Diversity of group types, regulation, and function of phospholipase A2. J. Biol. Chem. 269 (1994) 13057-13060
    • (1994) J. Biol. Chem. , vol.269 , pp. 13057-13060
    • Dennis, E.A.1
  • 4
    • 33751028489 scopus 로고    scopus 로고
    • The phospholipase A2 superfamily and its group numbering system
    • Schaloske R.H., and Dennis E.A. The phospholipase A2 superfamily and its group numbering system. Biochim. Biophys. Acta 1761 (2006) 1246-1259
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1246-1259
    • Schaloske, R.H.1    Dennis, E.A.2
  • 5
    • 0035222529 scopus 로고    scopus 로고
    • Diversity and regulatory functions of mammalian secretory phospholipases A2
    • Murakami M., and Kudo I. Diversity and regulatory functions of mammalian secretory phospholipases A2. Adv. Immunol. 77 (2001) 163-194
    • (2001) Adv. Immunol. , vol.77 , pp. 163-194
    • Murakami, M.1    Kudo, I.2
  • 6
    • 0030798853 scopus 로고    scopus 로고
    • A reassessment of the low molecular weight phospholipase A2 gene family in mammals
    • Tischfield J.A. A reassessment of the low molecular weight phospholipase A2 gene family in mammals. J. Biol. Chem. 272 (1997) 17247-17250
    • (1997) J. Biol. Chem. , vol.272 , pp. 17247-17250
    • Tischfield, J.A.1
  • 7
    • 0034739474 scopus 로고    scopus 로고
    • Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins
    • Valentin E., and Lambeau G. Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins. Biochim. Biophys. Acta 1488 (2000) 59-70
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 59-70
    • Valentin, E.1    Lambeau, G.2
  • 8
    • 0025923332 scopus 로고
    • Induction of phospholipase A2 gene expression in human hepatoma cells by mediators of the acute phase response
    • Crowl R.M., Stoller T.J., Conroy R.R., and Stoner C.R. Induction of phospholipase A2 gene expression in human hepatoma cells by mediators of the acute phase response. J. Biol. Chem. 266 (1991) 2647-2651
    • (1991) J. Biol. Chem. , vol.266 , pp. 2647-2651
    • Crowl, R.M.1    Stoller, T.J.2    Conroy, R.R.3    Stoner, C.R.4
  • 9
    • 0027473524 scopus 로고
    • Molecular nature of phospholipases A2 involved in prostaglandin I2 synthesis in human umbilical vein endothelial cells. Possible participation of cytosolic and extracellular type II phospholipases A2
    • Murakami M., Kudo I., and Inoue K. Molecular nature of phospholipases A2 involved in prostaglandin I2 synthesis in human umbilical vein endothelial cells. Possible participation of cytosolic and extracellular type II phospholipases A2. J. Biol. Chem. 268 (1993) 839-844
    • (1993) J. Biol. Chem. , vol.268 , pp. 839-844
    • Murakami, M.1    Kudo, I.2    Inoue, K.3
  • 12
    • 0027934181 scopus 로고
    • Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2
    • Chen J., Engle S.J., Seilhamer J.J., and Tischfield J.A. Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J. Biol. Chem. 269 (1994) 2365-2368
    • (1994) J. Biol. Chem. , vol.269 , pp. 2365-2368
    • Chen, J.1    Engle, S.J.2    Seilhamer, J.J.3    Tischfield, J.A.4
  • 13
    • 0029753778 scopus 로고    scopus 로고
    • Novel group V phospholipase A2 involved in arachidonic acid mobilization in murine P388D1 macrophages
    • Balboa M.A., Balsinde J., Winstead M.V., Tischfield J.A., and Dennis E.A. Novel group V phospholipase A2 involved in arachidonic acid mobilization in murine P388D1 macrophages. J. Biol. Chem. 271 (1996) 32381-32384
    • (1996) J. Biol. Chem. , vol.271 , pp. 32381-32384
    • Balboa, M.A.1    Balsinde, J.2    Winstead, M.V.3    Tischfield, J.A.4    Dennis, E.A.5
  • 14
    • 0031010458 scopus 로고    scopus 로고
    • Analysis of the secretory phospholipase A2 that mediates prostaglandin production in mast cells
    • Reddy S.T., Winstead M.V., Tischfield J.A., and Herschman H.R. Analysis of the secretory phospholipase A2 that mediates prostaglandin production in mast cells. J. Biol. Chem. 272 (1997) 13591-13596
    • (1997) J. Biol. Chem. , vol.272 , pp. 13591-13596
    • Reddy, S.T.1    Winstead, M.V.2    Tischfield, J.A.3    Herschman, H.R.4
  • 15
    • 0030905731 scopus 로고    scopus 로고
    • Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2
    • Cupillard L., Koumanov K., Mattei M.G., Lazdunski M., and Lambeau G. Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J. Biol. Chem. 272 (1997) 15745-15752
    • (1997) J. Biol. Chem. , vol.272 , pp. 15745-15752
    • Cupillard, L.1    Koumanov, K.2    Mattei, M.G.3    Lazdunski, M.4    Lambeau, G.5
  • 16
    • 0017484255 scopus 로고
    • Antigen-induced arthritis in mice. I. Induction of arthritis in various strains of mice
    • Brackertz D., Mitchell G.F., and Mackay I.R. Antigen-induced arthritis in mice. I. Induction of arthritis in various strains of mice. Arthritis Rheum. 20 (1977) 841-850
    • (1977) Arthritis Rheum. , vol.20 , pp. 841-850
    • Brackertz, D.1    Mitchell, G.F.2    Mackay, I.R.3
  • 17
    • 0021943982 scopus 로고
    • Type II collagen-induced arthritis in mice. III. Suppression of arthritis by using monoclonal and polyclonal anti-Ia antisera
    • Wooley P.H., Luthra H.S., Lafuse W.P., Huse A., Stuart J.M., and David C.S. Type II collagen-induced arthritis in mice. III. Suppression of arthritis by using monoclonal and polyclonal anti-Ia antisera. J. Immunol. 134 (1985) 2366-2374
    • (1985) J. Immunol. , vol.134 , pp. 2366-2374
    • Wooley, P.H.1    Luthra, H.S.2    Lafuse, W.P.3    Huse, A.4    Stuart, J.M.5    David, C.S.6
  • 18
    • 17144425052 scopus 로고    scopus 로고
    • Phospholipases A2: structure and function
    • Wilton D.C. Phospholipases A2: structure and function. Eur. J. Lipid Sci. Technol. 107 (2005) 193-205
    • (2005) Eur. J. Lipid Sci. Technol. , vol.107 , pp. 193-205
    • Wilton, D.C.1
  • 20
    • 0021364597 scopus 로고
    • Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins
    • Thannhauser T.W., Konishi Y., and Scheraga H.A. Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins. Anal. Biochem. 138 (1984) 181-188
    • (1984) Anal. Biochem. , vol.138 , pp. 181-188
    • Thannhauser, T.W.1    Konishi, Y.2    Scheraga, H.A.3
  • 21
    • 0034961960 scopus 로고    scopus 로고
    • Refolding and purification of Bothropstoxin-I, a Lys49-phospholipase A2 homologue, expressed as inclusion bodies in Escherichia coli
    • Ward R.J., de Oliveira A.H., Bortoleto R.K., Rosa J.C., Faca V.M., and Greene L.J. Refolding and purification of Bothropstoxin-I, a Lys49-phospholipase A2 homologue, expressed as inclusion bodies in Escherichia coli. Protein Expres. Purif. 21 (2001) 134-140
    • (2001) Protein Expres. Purif. , vol.21 , pp. 134-140
    • Ward, R.J.1    de Oliveira, A.H.2    Bortoleto, R.K.3    Rosa, J.C.4    Faca, V.M.5    Greene, L.J.6
  • 22
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chacon P., Merelo J.J., and Moran F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6 (1993) 383-390
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 23
    • 0032904864 scopus 로고    scopus 로고
    • The measurement of free fatty acid concentration with the fluorescent probe ADIFAB: a practical guide for the use of the ADIFAB probe
    • Richieri G.V., Ogata R.T., and Kleinfeld A.M. The measurement of free fatty acid concentration with the fluorescent probe ADIFAB: a practical guide for the use of the ADIFAB probe. Mol. Cell. Biochem. 192 (1999) 87-94
    • (1999) Mol. Cell. Biochem. , vol.192 , pp. 87-94
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 24
    • 47749112015 scopus 로고    scopus 로고
    • Insights on calcium-independent phospholipid membrane damage by Lys49-PLA2 using tryptophan scanning mutagenesis of bothropstoxin-I from Bothrops jararacussu
    • Ferreira T.L., Ruller R., Chioato L., and Ward R.J. Insights on calcium-independent phospholipid membrane damage by Lys49-PLA2 using tryptophan scanning mutagenesis of bothropstoxin-I from Bothrops jararacussu. Biochimie 90 (2008) 1397-1406
    • (2008) Biochimie , vol.90 , pp. 1397-1406
    • Ferreira, T.L.1    Ruller, R.2    Chioato, L.3    Ward, R.J.4
  • 25
    • 67650152452 scopus 로고    scopus 로고
    • L. Chioato, Investigação das bases estruturais das atividades de bothropstoxina-I, uma fosfolipase A2-Lis49 isolada do veneno de Bothrops jararacussu e da fosfolipase A2 secretada humana do grupo IIA, Bioquímica e Imunologia, FMRP-USP, Ribeirão Preto-SP, 2004, p. 188.
    • L. Chioato, Investigação das bases estruturais das atividades de bothropstoxina-I, uma fosfolipase A2-Lis49 isolada do veneno de Bothrops jararacussu e da fosfolipase A2 secretada humana do grupo IIA, Bioquímica e Imunologia, FMRP-USP, Ribeirão Preto-SP, 2004, p. 188.
  • 26
    • 40449120021 scopus 로고    scopus 로고
    • Permeabilization of E. coli K12 inner and outer membranes by bothropstoxin-I, A LYS49 phospholipase A2 from Bothrops jararacussu
    • Aragao E.A., Chioato L., and Ward R.J. Permeabilization of E. coli K12 inner and outer membranes by bothropstoxin-I, A LYS49 phospholipase A2 from Bothrops jararacussu. Toxicon 51 (2008) 538-546
    • (2008) Toxicon , vol.51 , pp. 538-546
    • Aragao, E.A.1    Chioato, L.2    Ward, R.J.3
  • 27
    • 0026342821 scopus 로고
    • Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate
    • Scott D.L., White S.P., Browning J.L., Rosa J.J., Gelb M.H., and Sigler P.B. Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science 254 (1991) 1007-1010
    • (1991) Science , vol.254 , pp. 1007-1010
    • Scott, D.L.1    White, S.P.2    Browning, J.L.3    Rosa, J.J.4    Gelb, M.H.5    Sigler, P.B.6
  • 28
    • 0032750764 scopus 로고    scopus 로고
    • Considerations of sample application and elution during size-exclusion chromatography-based protein refolding
    • Batas B., and Chaudhuri J.B. Considerations of sample application and elution during size-exclusion chromatography-based protein refolding. J. Chromatogr. A 864 (1998) 229-236
    • (1998) J. Chromatogr. A , vol.864 , pp. 229-236
    • Batas, B.1    Chaudhuri, J.B.2
  • 29
    • 0033023784 scopus 로고    scopus 로고
    • Inclusion body purification and protein refolding using microfiltration and size exclusion chromatography
    • Batas B., Schiraldi C., and Chaudhuri J.B. Inclusion body purification and protein refolding using microfiltration and size exclusion chromatography. J. Biotechnol. 68 (1999) 149-158
    • (1999) J. Biotechnol. , vol.68 , pp. 149-158
    • Batas, B.1    Schiraldi, C.2    Chaudhuri, J.B.3
  • 30
    • 0028358009 scopus 로고
    • Structure and catalytic mechanism of secretory phospholipases A2
    • Scott D.L., and Sigler P.B. Structure and catalytic mechanism of secretory phospholipases A2. Adv. Protein Chem. 45 (1994) 53-58
    • (1994) Adv. Protein Chem. , vol.45 , pp. 53-58
    • Scott, D.L.1    Sigler, P.B.2
  • 31
    • 0031745866 scopus 로고    scopus 로고
    • A sequence space analysis of Lys49 phopholipases A2: clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity
    • Ward R.J., Alves A.R., Ruggiero Neto J., Arni R.K., and Casari G. A sequence space analysis of Lys49 phopholipases A2: clues towards identification of residues involved in a novel mechanism of membrane damage and in myotoxicity. Protein Eng. 11 (1998) 285-294
    • (1998) Protein Eng. , vol.11 , pp. 285-294
    • Ward, R.J.1    Alves, A.R.2    Ruggiero Neto, J.3    Arni, R.K.4    Casari, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.