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Volumn 22, Issue 2, 2009, Pages 104-109

Characterization of multimodal hydrophobic interaction chromatography media useful for isolation of green fluorescent proteins with small structural differences

Author keywords

Green fluorescent protein; Hydrophobic interaction chromatography; pH responsive; Polymer ligand; Tyrosine tag

Indexed keywords

ESCHERICHIA;

EID: 63449090356     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.897     Document Type: Article
Times cited : (12)

References (23)
  • 1
    • 0034705818 scopus 로고    scopus 로고
    • Partitioning of peptides and recombinant protein-peptide fusions in thermoseparating aqueous two-phase systems: Effect of peptide primary structure
    • Berggren K, Nilsson A, Johansson G, Bandmann N, Nygren P, Tjerneld F, 2000. Partitioning of peptides and recombinant protein-peptide fusions in thermoseparating aqueous two-phase systems: effect of peptide primary structure, J. Chromatogr. B Biomed. Sci. Appl. 743: 295-306.
    • (2000) J. Chromatogr. B Biomed. Sci. Appl , vol.743 , pp. 295-306
    • Berggren, K.1    Nilsson, A.2    Johansson, G.3    Bandmann, N.4    Nygren, P.5    Tjerneld, F.6
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram 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
  • 3
    • 63849266037 scopus 로고    scopus 로고
    • CAMO, CAMO PROCESS AS. 2005. Nedre Vollgate 8, N-0158 Oslo, Norway.
    • CAMO, CAMO PROCESS AS. 2005. Nedre Vollgate 8, N-0158 Oslo, Norway.
  • 4
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A, Whitehorn EA, Tate E, Stemmer WPC. 1996. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14(3): 315-319.
    • (1996) Nat. Biotechnol , vol.14 , Issue.3 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.C.4
  • 5
    • 0023059404 scopus 로고
    • Solute and mobile phase contributions to retention in hydrophobic interaction chromatography of proteins
    • Fausnaugh JL, Regnier FE. 1986, Solute and mobile phase contributions to retention in hydrophobic interaction chromatography of proteins. J. Chromatogr. 359: 131-146.
    • (1986) J. Chromatogr , vol.359 , pp. 131-146
    • Fausnaugh, J.L.1    Regnier, F.E.2
  • 6
    • 0036421610 scopus 로고    scopus 로고
    • Improved partitioning in aqueous two-phase system of tyrosine-tagged recombinant lactate dehydrogenase
    • Fexby S, Bülow L. 2002. Improved partitioning in aqueous two-phase system of tyrosine-tagged recombinant lactate dehydrogenase. Protein Expr. Purif. 25: 263-269.
    • (2002) Protein Expr. Purif , vol.25 , pp. 263-269
    • Fexby, S.1    Bülow, L.2
  • 7
    • 2942704125 scopus 로고    scopus 로고
    • Partitioning and characterization of tyrosine-tagged green fluorescent proteins in aqueous two-phase systems
    • Fexby S, Nilsson A, Hambraeus G, Tjerneld F, Bülow L. 2004. Partitioning and characterization of tyrosine-tagged green fluorescent proteins in aqueous two-phase systems. Biotechnol. Prog. 20: 793-798.
    • (2004) Biotechnol. Prog , vol.20 , pp. 793-798
    • Fexby, S.1    Nilsson, A.2    Hambraeus, G.3    Tjerneld, F.4    Bülow, L.5
  • 8
    • 28144463212 scopus 로고    scopus 로고
    • Development and scale up of preparative HIC for the purification of a recombinant therapeutic protein
    • Graumann K, Ebenbichler AA. 2005. Development and scale up of preparative HIC for the purification of a recombinant therapeutic protein. Chem. Eng. Technol. 28(11): 1398-1407.
    • (2005) Chem. Eng. Technol , vol.28 , Issue.11 , pp. 1398-1407
    • Graumann, K.1    Ebenbichler, A.A.2
  • 9
    • 0028235493 scopus 로고
    • Polyethylene-glycol-potassium phosphate aqueous two-phase systems. Insertion of short peptide units into a protein and its effects on partitioning
    • Hassinen C, Köhler K, Veide A. 1994. Polyethylene-glycol-potassium phosphate aqueous two-phase systems. Insertion of short peptide units into a protein and its effects on partitioning. J. Chromatogr. A 668: 121-128.
    • (1994) J. Chromatogr. A , vol.668 , pp. 121-128
    • Hassinen, C.1    Köhler, K.2    Veide, A.3
  • 11
    • 28144436889 scopus 로고    scopus 로고
    • Prediction protein retention in hydrophobic interaction chromatography
    • Lienqueo ME, Mahn A. 2005. Prediction protein retention in hydrophobic interaction chromatography. Chem. Eng. Technol. 28(11): 1326- 1334.
    • (2005) Chem. Eng. Technol , vol.28 , Issue.11 , pp. 1326-1334
    • Lienqueo, M.E.1    Mahn, A.2
  • 12
    • 33646125859 scopus 로고    scopus 로고
    • Electrostatic calculations and quantitative protein retention models for ion exchange chromatography
    • Malmquist G, Nilsson U, Norrman M, Skarp U, Strömgren M, Carredano E. 2006. Electrostatic calculations and quantitative protein retention models for ion exchange chromatography. J. Chromatogr. A 1115: 164-186.
    • (2006) J. Chromatogr. A , vol.1115 , pp. 164-186
    • Malmquist, G.1    Nilsson, U.2    Norrman, M.3    Skarp, U.4    Strömgren, M.5    Carredano, E.6
  • 13
    • 15744368360 scopus 로고    scopus 로고
    • Rapid purification of EGFP, EYFP, and ECFP with high yield and purity
    • McRae SR, Brown CL, Bushell GR. 2005. Rapid purification of EGFP, EYFP, and ECFP with high yield and purity. Protein Expr. Purif. 41: 121 - 127.
    • (2005) Protein Expr. Purif , vol.41 , pp. 121-127
    • McRae, S.R.1    Brown, C.L.2    Bushell, G.R.3
  • 14
    • 0023772634 scopus 로고
    • Enzyme purification by genetically attached polycysteine and polyphenylalanine affinity tails
    • Persson M, Bergstrand M, Bülow L, Mosbach K. 1988. Enzyme purification by genetically attached polycysteine and polyphenylalanine affinity tails. Anal. Biochem. 172: 330-337.
    • (1988) Anal. Biochem , vol.172 , pp. 330-337
    • Persson, M.1    Bergstrand, M.2    Bülow, L.3    Mosbach, K.4
  • 15
    • 0034446067 scopus 로고    scopus 로고
    • Extraction of peptide tagged cutinase in detergent-based aqueous two-phase systems
    • Rodenbrock A, Selber K, Egmond MR, Kula MR. 2001, Extraction of peptide tagged cutinase in detergent-based aqueous two-phase systems. Bioseparation 9: 269-276.
    • (2001) Bioseparation , vol.9 , pp. 269-276
    • Rodenbrock, A.1    Selber, K.2    Egmond, M.R.3    Kula, M.R.4
  • 16
    • 27944496401 scopus 로고    scopus 로고
    • Prediction of retention times of proteins in hydrophobic interaction chromatography using only their amino acid composition
    • Salgado C, Rapaport I, Asenjo JA. 2005a, Prediction of retention times of proteins in hydrophobic interaction chromatography using only their amino acid composition. J. Chromatogr. A 1098: 44-54.
    • (2005) J. Chromatogr. A , vol.1098 , pp. 44-54
    • Salgado, C.1    Rapaport, I.2    Asenjo, J.A.3
  • 17
    • 19344368651 scopus 로고    scopus 로고
    • Is it possible to predict the average surface hydrophobicity of a protein using only its amino acid composition?
    • Salgado C, Rapaport I, Asenjo JA. 2005b, Is it possible to predict the average surface hydrophobicity of a protein using only its amino acid composition? J. Chromatogr. A 1075: 133-143.
    • (2005) J. Chromatogr. A , vol.1075 , pp. 133-143
    • Salgado, C.1    Rapaport, I.2    Asenjo, J.A.3
  • 18
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O, Johnson FH, Saiga Y, 1962, Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59: 223.
    • (1962) J. Cell. Comp. Physiol , vol.59 , pp. 223
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 19
    • 0347613015 scopus 로고    scopus 로고
    • Current and prospective applications of metal ion-protein binding
    • Ueda EKM, Gout PW, Morganti L. 2003. Current and prospective applications of metal ion-protein binding. J. Chromatogr. A 988: 1-23.
    • (2003) J. Chromatogr. A , vol.988 , pp. 1-23
    • Ueda, E.K.M.1    Gout, P.W.2    Morganti, L.3
  • 20
    • 0242320516 scopus 로고    scopus 로고
    • Yeast as a sensor of factors affecting the accuracy of protein synthesis
    • Valente L, Kinzy TG. 2003. Yeast as a sensor of factors affecting the accuracy of protein synthesis, Cell. Mol. Life Sci. 60: 2115-2130.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 2115-2130
    • Valente, L.1    Kinzy, T.G.2
  • 22
    • 0017135371 scopus 로고
    • On the mode of adsorption of proteins to "hydrophobic columns
    • Wilchek M, Miron T, 1976. On the mode of adsorption of proteins to "hydrophobic columns". Biochem. Biophys. Res. Commun. 72:108-113.
    • (1976) Biochem. Biophys. Res. Commun , vol.72 , pp. 108-113
    • Wilchek, M.1    Miron, T.2
  • 23
    • 0015298452 scopus 로고
    • Chromatography of lipophilic proteins on adsorbents containing mixed hydrophobic and ionic groups
    • Yon RJ. 1972. Chromatography of lipophilic proteins on adsorbents containing mixed hydrophobic and ionic groups, Biochem. J. 126: 765-767.
    • (1972) Biochem. J , vol.126 , pp. 765-767
    • Yon, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.