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Volumn 98, Issue 1, 2007, Pages 48-59

Production of synthetically created phospholipase A2 variants with industrial impact

Author keywords

Bee venom; Escherichia coli; High cell density fermentation inclusion bodies; Phospholipase A2; Renaturation

Indexed keywords

BIOSYNTHESIS; ESCHERICHIA COLI; GENE EXPRESSION; ION EXCHANGE; OPTIMIZATION; THERMODYNAMIC STABILITY;

EID: 34548266808     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21392     Document Type: Article
Times cited : (10)

References (44)
  • 2
    • 0033168903 scopus 로고    scopus 로고
    • Quantitative protein precipitation from guanidine hydrochloride-containing solutions by sodium deoxycholate/ trichloroacetic acid
    • Arnold U, Ulbrich-Hofmann R. 1999. Quantitative protein precipitation from guanidine hydrochloride-containing solutions by sodium deoxycholate/ trichloroacetic acid. Anal Biochem 271:197-199.
    • (1999) Anal Biochem , vol.271 , pp. 197-199
    • Arnold, U.1    Ulbrich-Hofmann, R.2
  • 3
    • 0037201940 scopus 로고    scopus 로고
    • Phospholipase A(2) regulation of arachidonic acid mobilization
    • Balsinde J, Winstead MV, Dennis EA. 2002. Phospholipase A(2) regulation of arachidonic acid mobilization. FEBS Lett 531:2-6.
    • (2002) FEBS Lett , vol.531 , pp. 2-6
    • Balsinde, J.1    Winstead, M.V.2    Dennis, E.A.3
  • 4
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. 1999. Recombinant protein expression in Escherichia coli. Curr Opin Biotech 10:411-421.
    • (1999) Curr Opin Biotech , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 5
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow DM, Birktoft JJ, Hartley BS. 1969. Role of a buried acid group in the mechanism of action of chymotrypsin. Nature 221:337-340.
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 6
    • 0037083053 scopus 로고    scopus 로고
    • Effect of operating variables on the yield of recombinant trypsinogen for a pulse-fed dilution-refolding reactor
    • Buswell AM, Ebtinger M, Vertes AA, Middelberg AP. 2002. Effect of operating variables on the yield of recombinant trypsinogen for a pulse-fed dilution-refolding reactor. Biotechnol Bioeng 77:435-444.
    • (2002) Biotechnol Bioeng , vol.77 , pp. 435-444
    • Buswell, A.M.1    Ebtinger, M.2    Vertes, A.A.3    Middelberg, A.P.4
  • 7
    • 0030598859 scopus 로고    scopus 로고
    • 2 in Escherichia coli, a fully active enzyme generated by hydrolyzing with aminopeptidase
    • 2 in Escherichia coli, a fully active enzyme generated by hydrolyzing with aminopeptidase. Biochem Biophys Res Commun 225:990-996.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 990-996
    • Chang, L.S.1    Wu, P.F.2    Chang, C.C.3
  • 9
    • 0029032586 scopus 로고
    • Engineering ribonuclease A: Production, purification and characterization of wild-type enzyme and mutants at Gln11
    • delCardayré SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. 1995. Engineering ribonuclease A: Production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng 8:261-273.
    • (1995) Protein Eng , vol.8 , pp. 261-273
    • delCardayré, S.B.1    Ribo, M.2    Yokel, E.M.3    Quirk, D.J.4    Rutter, W.J.5    Raines, R.T.6
  • 12
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink MR, Ghiron CA. 1976. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 15:672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 14
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert HF. 1990. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol 63:69-172.
    • (1990) Adv Enzymol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 19
    • 0025783513 scopus 로고
    • 2 from pancreas and venom using a continuous fluorescence displacement assay
    • 2 from pancreas and venom using a continuous fluorescence displacement assay. Biochem J 278:843-848.
    • (1991) Biochem J , vol.278 , pp. 843-848
    • Kinkaid, A.1    Wilton, D.C.2
  • 20
    • 0024726507 scopus 로고
    • 2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes
    • 2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes. Eur J Biochem 184:249-254.
    • (1989) Eur J Biochem , vol.184 , pp. 249-254
    • Kuchler, K.1    Gmachl, M.2    Sippl, M.J.3    Kreil, G.4
  • 22
    • 0027016691 scopus 로고
    • 2 from the venom of Agkistrodon piscivorus piscivorus in Escherichia coli: Recovery and renaturation from bacterial inclusion bodies
    • 2 from the venom of Agkistrodon piscivorus piscivorus in Escherichia coli: recovery and renaturation from bacterial inclusion bodies. Protein Expr Purif 3:512-517.
    • (1992) Protein Expr Purif , vol.3 , pp. 512-517
    • Lathrop, B.K.1    Burack, W.R.2    Biltonen, R.L.3    Rule, G.S.4
  • 23
    • 0036017860 scopus 로고    scopus 로고
    • Phospholipid signalling in plant defence
    • Laxalt AM, Munnik T. 2002. Phospholipid signalling in plant defence. Curr Opin Plant Biol 5:332-338.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 332-338
    • Laxalt, A.M.1    Munnik, T.2
  • 24
    • 0033607222 scopus 로고    scopus 로고
    • 2 in Pichia pastoris: Identification of a phosphatidylcholine activator site using site-directed mutagenesis
    • 2 in Pichia pastoris: Identification of a phosphatidylcholine activator site using site-directed mutagenesis. Biochemistry 38:14174-14184.
    • (1999) Biochemistry , vol.38 , pp. 14174-14184
    • Lefkowitz, L.J.1    Deems, R.A.2    Dennis, E.A.3
  • 25
    • 0023410604 scopus 로고
    • Characterization of the Erwinia carotovora pelB gene and its product pectate lyase
    • Lei SP, Lin HC, Wang SS, Callaway J, Wilcox G. 1987. Characterization of the Erwinia carotovora pelB gene and its product pectate lyase. J Bacteriol 169:4379-4383.
    • (1987) J Bacteriol , vol.169 , pp. 4379-4383
    • Lei, S.P.1    Lin, H.C.2    Wang, S.S.3    Callaway, J.4    Wilcox, G.5
  • 26
    • 0023802464 scopus 로고    scopus 로고
    • 2 from bovine pancreas and bee venom. J Biol Chem 263:13208-13214.
    • 2 from bovine pancreas and bee venom. J Biol Chem 263:13208-13214.
  • 28
    • 0015356276 scopus 로고
    • Further studies on the properties of phospholipase A from honeybee (Apis mellifera) venom
    • Munjal D, Elliott WB. 1972. Further studies on the properties of phospholipase A from honeybee (Apis mellifera) venom. Toxicon 10:367-375.
    • (1972) Toxicon , vol.10 , pp. 367-375
    • Munjal, D.1    Elliott, W.B.2
  • 32
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton TE, editor, IRL Press. Oxford: p
    • Pace CN, Shirley BA, Thomson JA. 1989. Measuring the conformational stability of a protein. In: Creighton TE, editor. Protein structure - a practical approach. IRL Press. Oxford: p 311-330.
    • (1989) Protein structure - a practical approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 35
    • 0022182544 scopus 로고
    • 2 and comparison with other phospholipases
    • 2 and comparison with other phospholipases. J Biol Chem 260:11099-11106.
    • (1985) J Biol Chem , vol.260 , pp. 11099-11106
    • Plückthun, A.1    Dennis, E.A.2
  • 39
    • 0034739463 scopus 로고    scopus 로고
    • 2 enzymes: Classification and characterization
    • 2 enzymes: Classification and characterization. Biochim Biophys Acta 1488:1-19.
    • (2000) Biochim Biophys Acta , vol.1488 , pp. 1-19
    • Six, D.A.1    Dennis, A.2
  • 40
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer WP, Crameri A, Ha KD, Brennan TM, Heyneker HL. 1995. Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164:49-53.
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 41
    • 0023949985 scopus 로고
    • 2 enzyme by Saccharomyces cerevisiae: Design and use of a synthetic gene
    • 2 enzyme by Saccharomyces cerevisiae: Design and use of a synthetic gene. Gene 64:257-264.
    • (1988) Gene , vol.64 , pp. 257-264
    • Tanaka, T.1    Kimura, S.2    Ota, Y.3
  • 42
    • 0001521873 scopus 로고    scopus 로고
    • Phospholipases used in lipid transformations
    • Bornscheuer UT, editor, Wiley-VCH. Weinheim: p
    • Ulbrich-Hofmann R. 2000. Phospholipases used in lipid transformations. In: Bornscheuer UT, editor. Enzymes in lipid modification. Wiley-VCH. Weinheim: p 219-262.
    • (2000) Enzymes in lipid modification , pp. 219-262
    • Ulbrich-Hofmann, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.