메뉴 건너뛰기




Volumn 28, Issue 5, 2010, Pages 272-279

The potential role of self-cleaving purification tags in commercial-scale processes

Author keywords

[No Author keywords available]

Indexed keywords

EMERGING TECHNOLOGIES; INTEINS; PLATFORM PROCESS; PURIFICATION TAGS; TAG REMOVAL; TARGET PROTEINS; WIDE SELECTION;

EID: 77951976127     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2010.02.003     Document Type: Review
Times cited : (76)

References (64)
  • 1
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • Arnau J., et al. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr. Purif. 2006, 48:1-13.
    • (2006) Protein Expr. Purif. , vol.48 , pp. 1-13
    • Arnau, J.1
  • 2
    • 15744372778 scopus 로고    scopus 로고
    • Comparison of affinity tags for protein purification
    • Lichty J.J., et al. Comparison of affinity tags for protein purification. Protein Expr. Purif. 2005, 41:98-105.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 98-105
    • Lichty, J.J.1
  • 3
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 2003, 60:523-533.
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 523-533
    • Terpe, K.1
  • 4
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh D.S. Making the most of affinity tags. Trends Biotechnol. 2005, 23:316-320.
    • (2005) Trends Biotechnol. , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 5
    • 0036421180 scopus 로고    scopus 로고
    • Expression of the class 1 outer-membrane protein of Neisseria meningitidis in Escherichia coli and purification using a self-cleavable affinity tag
    • Humphries H.E., et al. Expression of the class 1 outer-membrane protein of Neisseria meningitidis in Escherichia coli and purification using a self-cleavable affinity tag. Protein Expr. Purif. 2002, 26:243-248.
    • (2002) Protein Expr. Purif. , vol.26 , pp. 243-248
    • Humphries, H.E.1
  • 6
    • 23944463921 scopus 로고    scopus 로고
    • Simulation of large-scale production of a soluble recombinant protein expressed in Escherichia coli using an intein-mediated purification system
    • Sharma S.S., et al. Simulation of large-scale production of a soluble recombinant protein expressed in Escherichia coli using an intein-mediated purification system. Appl. Biochem. Biotechnol. 2005, 126:93-118.
    • (2005) Appl. Biochem. Biotechnol. , vol.126 , pp. 93-118
    • Sharma, S.S.1
  • 7
    • 0038648648 scopus 로고    scopus 로고
    • Crystal structures of fusion proteins with large-affinity tags
    • Smyth D.R., et al. Crystal structures of fusion proteins with large-affinity tags. Protein Sci. 2003, 12:1313-1322.
    • (2003) Protein Sci. , vol.12 , pp. 1313-1322
    • Smyth, D.R.1
  • 8
    • 0032757296 scopus 로고    scopus 로고
    • Natural poly-histidine affinity tag for purification of recombinant proteins on cobalt(II)-carboxymethylaspartate crosslinked agarose
    • Chaga G., et al. Natural poly-histidine affinity tag for purification of recombinant proteins on cobalt(II)-carboxymethylaspartate crosslinked agarose. J. Chromatogr. A 1999, 864:247-256.
    • (1999) J. Chromatogr. A , vol.864 , pp. 247-256
    • Chaga, G.1
  • 9
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins
    • Skerra A., Schmidt T.G. Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol. 2000, 326:271-304.
    • (2000) Methods Enzymol. , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.2
  • 10
    • 23844438834 scopus 로고    scopus 로고
    • Self-cleavable stimulus responsive tags for protein purification without chromatography
    • Ge X., et al. Self-cleavable stimulus responsive tags for protein purification without chromatography. J. Am. Chem. Soc. 2005, 127:11228-11229.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11228-11229
    • Ge, X.1
  • 11
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastin-like polypeptide tags
    • Banki M.R., et al. Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nat. Methods 2005, 2:659-661.
    • (2005) Nat. Methods , vol.2 , pp. 659-661
    • Banki, M.R.1
  • 12
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • Meyer D.E., Chilkoti A. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 1999, 17:1112-1115.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 13
    • 34548841392 scopus 로고    scopus 로고
    • Recombinant protein purification by self-cleaving aggregation tag
    • Wu W.Y., et al. Recombinant protein purification by self-cleaving aggregation tag. Nat. Protoc. 2006, 1:2257-2262.
    • (2006) Nat. Protoc. , vol.1 , pp. 2257-2262
    • Wu, W.Y.1
  • 14
    • 2542628131 scopus 로고    scopus 로고
    • Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides
    • Meyer D.E., Chilkoti A. Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides. Biomacromolecules 2004, 5:846-851.
    • (2004) Biomacromolecules , vol.5 , pp. 846-851
    • Meyer, D.E.1    Chilkoti, A.2
  • 15
    • 0023953406 scopus 로고
    • Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics
    • Urry D.W. Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics. J. Protein Chem. 1988, 7:1-34.
    • (1988) J. Protein Chem. , vol.7 , pp. 1-34
    • Urry, D.W.1
  • 16
    • 0038388786 scopus 로고    scopus 로고
    • Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers
    • Urry D.W. Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers. J. Phys. Chem. B 1997, 101:11007-11028.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 11007-11028
    • Urry, D.W.1
  • 17
    • 0026926763 scopus 로고
    • Hydrophobicity scale for proteins based on inverse temperature transitions
    • Urry D.W., et al. Hydrophobicity scale for proteins based on inverse temperature transitions. Biopolymers 1992, 32:1243-1250.
    • (1992) Biopolymers , vol.32 , pp. 1243-1250
    • Urry, D.W.1
  • 18
    • 28144460981 scopus 로고    scopus 로고
    • Inteins and affinity resin substitutes for protein purification and scale up
    • Banki M.R., Wood D.W. Inteins and affinity resin substitutes for protein purification and scale up. Microb. Cell Fact. 2005, 4:32.
    • (2005) Microb. Cell Fact. , vol.4 , pp. 32
    • Banki, M.R.1    Wood, D.W.2
  • 19
    • 9344234999 scopus 로고    scopus 로고
    • Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion
    • Trabbic-Carlson K., et al. Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion. Protein Sci. 2004, 13:3274-3284.
    • (2004) Protein Sci. , vol.13 , pp. 3274-3284
    • Trabbic-Carlson, K.1
  • 20
    • 65549096684 scopus 로고    scopus 로고
    • Optimization of elastin-like polypeptide fusions for expression and purification of recombinant proteins in plants
    • Conley A.J., et al. Optimization of elastin-like polypeptide fusions for expression and purification of recombinant proteins in plants. Biotechnol. Bioeng. 2009, 103:562-573.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 562-573
    • Conley, A.J.1
  • 21
    • 33748747042 scopus 로고    scopus 로고
    • Functional expression of a biologically active fragment of soluble gp130 as an ELP-fusion protein in transgenic plants: purification via inverse transition cycling
    • Lin M., et al. Functional expression of a biologically active fragment of soluble gp130 as an ELP-fusion protein in transgenic plants: purification via inverse transition cycling. Biochem. J. 2006, 398:577-583.
    • (2006) Biochem. J. , vol.398 , pp. 577-583
    • Lin, M.1
  • 22
    • 22444444258 scopus 로고    scopus 로고
    • Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
    • Banki M.R., et al. Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Sci. 2005, 14:1387-1395.
    • (2005) Protein Sci. , vol.14 , pp. 1387-1395
    • Banki, M.R.1
  • 23
    • 26844545316 scopus 로고    scopus 로고
    • Integrated recombinant protein expression and purification platform based on Ralstonia eutropha
    • Barnard G.C., et al. Integrated recombinant protein expression and purification platform based on Ralstonia eutropha. Appl. Environ. Microbiol. 2005, 71:5735-5742.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5735-5742
    • Barnard, G.C.1
  • 24
    • 2942558481 scopus 로고    scopus 로고
    • In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF
    • Moldes C., et al. In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF. Appl. Environ. Microbiol. 2004, 70:3205-3212.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3205-3212
    • Moldes, C.1
  • 25
    • 54349115910 scopus 로고    scopus 로고
    • A novel self-cleaving phasin tag for purification of recombinant proteins based on hydrophobic polyhydroxyalkanoate nanoparticles
    • Wang Z., et al. A novel self-cleaving phasin tag for purification of recombinant proteins based on hydrophobic polyhydroxyalkanoate nanoparticles. Lab Chip 2008, 8:1957-1962.
    • (2008) Lab Chip , vol.8 , pp. 1957-1962
    • Wang, Z.1
  • 26
    • 35649017202 scopus 로고    scopus 로고
    • A novel, cheap and effective fusion expression system for the production of recombinant proteins
    • Ding F.X., et al. A novel, cheap and effective fusion expression system for the production of recombinant proteins. Appl. Microbiol. Biotechnol. 2007, 77:483-488.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 483-488
    • Ding, F.X.1
  • 27
    • 1442338396 scopus 로고    scopus 로고
    • Non-fusion expression in Escherichia coli, purification, and characterization of a novel Ca2+- and phospholipid-binding protein annexin B1
    • Zhang Y., et al. Non-fusion expression in Escherichia coli, purification, and characterization of a novel Ca2+- and phospholipid-binding protein annexin B1. Protein Expr. Purif. 2004, 34:68-74.
    • (2004) Protein Expr. Purif. , vol.34 , pp. 68-74
    • Zhang, Y.1
  • 28
    • 34249903605 scopus 로고    scopus 로고
    • Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides
    • Lim D.W., et al. Improved non-chromatographic purification of a recombinant protein by cationic elastin-like polypeptides. Biomacromolecules 2007, 8:1417-1424.
    • (2007) Biomacromolecules , vol.8 , pp. 1417-1424
    • Lim, D.W.1
  • 29
    • 0028214350 scopus 로고
    • Protein splicing elements: inteins and exteins-a definition of terms and recommended nomenclature
    • Perler F.B., et al. Protein splicing elements: inteins and exteins-a definition of terms and recommended nomenclature. Nucleic Acids Res. 1994, 22:1125-1127.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1125-1127
    • Perler, F.B.1
  • 30
    • 0032534048 scopus 로고    scopus 로고
    • Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step
    • Chong S., et al. Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step. Nucleic Acids Res. 1998, 26:5109-5115.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5109-5115
    • Chong, S.1
  • 31
    • 0036405356 scopus 로고    scopus 로고
    • Inteins: structure, function, and evolution
    • Gogarten J.P., et al. Inteins: structure, function, and evolution. Annu. Rev. Microbiol. 2002, 56:263-287.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 263-287
    • Gogarten, J.P.1
  • 32
    • 0029834656 scopus 로고    scopus 로고
    • Protein splicing involving the Saccharomyces cerevisiae VMA intein. The steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system
    • Chong S., et al. Protein splicing involving the Saccharomyces cerevisiae VMA intein. The steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system. J. Biol. Chem. 1996, 271:22159-22168.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22159-22168
    • Chong, S.1
  • 33
    • 0026462996 scopus 로고
    • Mutations at the putative junction sites of the yeast VMA1 protein, the catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its processing by protein splicing
    • Hirata R., Anraku Y. Mutations at the putative junction sites of the yeast VMA1 protein, the catalytic subunit of the vacuolar membrane H(+)-ATPase, inhibit its processing by protein splicing. Biochem. Biophys. Res. Commun. 1992, 188:40-47.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 40-47
    • Hirata, R.1    Anraku, Y.2
  • 34
    • 0033614484 scopus 로고    scopus 로고
    • Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: facile production of protein building blocks for protein ligation
    • Mathys S., et al. Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: facile production of protein building blocks for protein ligation. Gene 1999, 231:1-13.
    • (1999) Gene , vol.231 , pp. 1-13
    • Mathys, S.1
  • 35
    • 0034518359 scopus 로고    scopus 로고
    • Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor
    • Wood D.W., et al. Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor. Biotechnol. Prog. 2000, 16:1055-1063.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 1055-1063
    • Wood, D.W.1
  • 36
    • 0032832776 scopus 로고    scopus 로고
    • A genetic system yields self-cleaving inteins for bioseparations
    • Wood D.W., et al. A genetic system yields self-cleaving inteins for bioseparations. Nat. Biotechnol. 1999, 17:889-892.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 889-892
    • Wood, D.W.1
  • 37
    • 0027984269 scopus 로고
    • Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation
    • Xu M.Q., et al. Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation. EMBO J. 1994, 13:5517-5522.
    • (1994) EMBO J. , vol.13 , pp. 5517-5522
    • Xu, M.Q.1
  • 38
    • 47749156371 scopus 로고    scopus 로고
    • Production of recombinant human epidermal growth factor using Ssp dnaB mini-intein system
    • Esipov R.S., et al. Production of recombinant human epidermal growth factor using Ssp dnaB mini-intein system. Protein Expr. Purif. 2008, 61:1-6.
    • (2008) Protein Expr. Purif. , vol.61 , pp. 1-6
    • Esipov, R.S.1
  • 39
    • 33745991799 scopus 로고    scopus 로고
    • Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli
    • Sharma S.S., et al. Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli. J. Biotechnol. 2006, 125:48-56.
    • (2006) J. Biotechnol. , vol.125 , pp. 48-56
    • Sharma, S.S.1
  • 40
    • 37449032617 scopus 로고    scopus 로고
    • Purification of green fluorescent protein using a two-intein system
    • Zhao Z., et al. Purification of green fluorescent protein using a two-intein system. Appl. Microbiol. Biotechnol. 2008, 77:1175-1180.
    • (2008) Appl. Microbiol. Biotechnol. , vol.77 , pp. 1175-1180
    • Zhao, Z.1
  • 41
    • 44349158280 scopus 로고    scopus 로고
    • Simple protein purification through affinity adsorption on regenerated amorphous cellulose followed by intein self-cleavage
    • Hong J., et al. Simple protein purification through affinity adsorption on regenerated amorphous cellulose followed by intein self-cleavage. J. Chromatogr. A 2008, 1194:150-154.
    • (2008) J. Chromatogr. A , vol.1194 , pp. 150-154
    • Hong, J.1
  • 42
    • 51649125516 scopus 로고    scopus 로고
    • Rapid cloning and purification of proteins: gateway vectors for protein purification by self-cleaving tags
    • Gillies A.R., et al. Rapid cloning and purification of proteins: gateway vectors for protein purification by self-cleaving tags. Biotechnol. Bioeng. 2008, 101:229-240.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 229-240
    • Gillies, A.R.1
  • 43
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element
    • Chong S., et al. Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 1997, 192:271-281.
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1
  • 44
    • 0034965749 scopus 로고    scopus 로고
    • Intein-mediated rapid purification of Cre recombinase
    • Cantor E.J., Chong S. Intein-mediated rapid purification of Cre recombinase. Protein Expr. Purif. 2001, 22:135-140.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 135-140
    • Cantor, E.J.1    Chong, S.2
  • 45
    • 0035913755 scopus 로고    scopus 로고
    • Construction of a mini-intein fusion system to allow both direct monitoring of soluble protein expression and rapid purification of target proteins
    • Zhang A., et al. Construction of a mini-intein fusion system to allow both direct monitoring of soluble protein expression and rapid purification of target proteins. Gene 2001, 275:241-252.
    • (2001) Gene , vol.275 , pp. 241-252
    • Zhang, A.1
  • 46
    • 37349023278 scopus 로고    scopus 로고
    • Construction of intein-mediated hGMCSF expression vector and its purification in Pichia pastoris
    • Babu K., et al. Construction of intein-mediated hGMCSF expression vector and its purification in Pichia pastoris. Protein Expr. Purif. 2008, 57:201-205.
    • (2008) Protein Expr. Purif. , vol.57 , pp. 201-205
    • Babu, K.1
  • 47
    • 2942620151 scopus 로고    scopus 로고
    • A novel " clip-and-link" activity of repeat in toxin (RTX) proteins from gram-negative pathogens. Covalent protein cross-linking by an Asp-Lys isopeptide bond upon calcium-dependent processing at an Asp-Pro bond
    • Osicka R., et al. A novel " clip-and-link" activity of repeat in toxin (RTX) proteins from gram-negative pathogens. Covalent protein cross-linking by an Asp-Lys isopeptide bond upon calcium-dependent processing at an Asp-Pro bond. J. Biol. Chem. 2004, 279:24944-24956.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24944-24956
    • Osicka, R.1
  • 48
    • 52949085497 scopus 로고    scopus 로고
    • Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC
    • Sadilkova L., et al. Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC. Protein Sci. 2008, 17:1834-1843.
    • (2008) Protein Sci. , vol.17 , pp. 1834-1843
    • Sadilkova, L.1
  • 49
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian S.K., et al. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 1999, 285:760-763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1
  • 50
    • 1542317850 scopus 로고    scopus 로고
    • Sortase-mediated protein ligation: a new method for protein engineering
    • Mao H., et al. Sortase-mediated protein ligation: a new method for protein engineering. J. Am. Chem. Soc. 2004, 126:2670-2671.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2670-2671
    • Mao, H.1
  • 51
    • 3543063548 scopus 로고    scopus 로고
    • A self-cleavable sortase fusion for one-step purification of free recombinant proteins
    • Mao H. A self-cleavable sortase fusion for one-step purification of free recombinant proteins. Protein Expr. Purif. 2004, 37:253-263.
    • (2004) Protein Expr. Purif. , vol.37 , pp. 253-263
    • Mao, H.1
  • 52
    • 1042288291 scopus 로고    scopus 로고
    • Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA
    • Kruger R.G., et al. Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA. Biochemistry 2004, 43:1541-1551.
    • (2004) Biochemistry , vol.43 , pp. 1541-1551
    • Kruger, R.G.1
  • 53
    • 34648828739 scopus 로고    scopus 로고
    • Cloning strategy, production and purification of proteins with exopeptidase-cleavable His-tags
    • Arnau J., et al. Cloning strategy, production and purification of proteins with exopeptidase-cleavable His-tags. Nat. Protoc. 2006, 1:2326-2333.
    • (2006) Nat. Protoc. , vol.1 , pp. 2326-2333
    • Arnau, J.1
  • 54
    • 0033117468 scopus 로고    scopus 로고
    • Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases
    • Pedersen J., et al. Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases. Protein Expr. Purif. 1999, 15:389-400.
    • (1999) Protein Expr. Purif. , vol.15 , pp. 389-400
    • Pedersen, J.1
  • 55
    • 77951978302 scopus 로고
    • A Process for Producing Human Growth Hormone
    • European Patent EP0217814, filed 02/06/1986, publication date 12/21/1994
    • Andersen, H., Dalboge, et al. (1994) A Process for Producing Human Growth Hormone. European Patent EP0217814, filed 02/06/1986, publication date 12/21/1994.
    • (1994)
    • Andersen, H.1    Dalboge2
  • 56
    • 0029740605 scopus 로고    scopus 로고
    • Human insulin: basic sciences to therapeutic uses
    • Chien Y.W. Human insulin: basic sciences to therapeutic uses. Drug Dev. Ind. Pharm. 1996, 22:753-789.
    • (1996) Drug Dev. Ind. Pharm. , vol.22 , pp. 753-789
    • Chien, Y.W.1
  • 57
    • 0032988320 scopus 로고    scopus 로고
    • Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein
    • Southworth M.W., et al. Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques 1999, 27:110-120.
    • (1999) Biotechniques , vol.27 , pp. 110-120
    • Southworth, M.W.1
  • 58
    • 0037157179 scopus 로고    scopus 로고
    • Production of a recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system
    • Morassutti C., et al. Production of a recombinant antimicrobial peptide in transgenic plants using a modified VMA intein expression system. FEBS Lett. 2002, 519:141-146.
    • (2002) FEBS Lett. , vol.519 , pp. 141-146
    • Morassutti, C.1
  • 59
    • 0032722062 scopus 로고    scopus 로고
    • Recombinant human DNA (cytosine-5) methyltransferase. I. Expression, purification, and comparison of de novo and maintenance methylation
    • Pradhan S., et al. Recombinant human DNA (cytosine-5) methyltransferase. I. Expression, purification, and comparison of de novo and maintenance methylation. J. Biol. Chem. 1999, 274:33002-33010.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33002-33010
    • Pradhan, S.1
  • 60
    • 0032122306 scopus 로고    scopus 로고
    • Antibody engineering: comparison of bacterial, yeast, insect and mammalian expression systems
    • Verma R., et al. Antibody engineering: comparison of bacterial, yeast, insect and mammalian expression systems. J. Immunol. Methods 1998, 216:165-181.
    • (1998) J. Immunol. Methods , vol.216 , pp. 165-181
    • Verma, R.1
  • 61
    • 0021991801 scopus 로고
    • The synthesis and in vivo assembly of functional antibodies in yeast
    • Wood C.R., et al. The synthesis and in vivo assembly of functional antibodies in yeast. Nature 1985, 314:446-449.
    • (1985) Nature , vol.314 , pp. 446-449
    • Wood, C.R.1
  • 62
    • 0029392471 scopus 로고
    • Production of human insulin in an E. coli system with Met-Lys-human proinsulin as the expressed precursor
    • Chen J.Q., et al. Production of human insulin in an E. coli system with Met-Lys-human proinsulin as the expressed precursor. Appl. Biochem. Biotechnol. 1995, 55:5-15.
    • (1995) Appl. Biochem. Biotechnol. , vol.55 , pp. 5-15
    • Chen, J.Q.1
  • 63
    • 34248202284 scopus 로고    scopus 로고
    • Intein-mediated expression is an effective approach in the study of beta-defensins
    • Diao H., et al. Intein-mediated expression is an effective approach in the study of beta-defensins. Biochem. Biophys. Res. Commun. 2007, 357:840-846.
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 840-846
    • Diao, H.1
  • 64
    • 67349157562 scopus 로고    scopus 로고
    • Optimization of ELP-intein mediated protein purification by salt substitution
    • Fong B.A., et al. Optimization of ELP-intein mediated protein purification by salt substitution. Protein Expr. Purif. 2009, 66:198-202.
    • (2009) Protein Expr. Purif. , vol.66 , pp. 198-202
    • Fong, B.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.