메뉴 건너뛰기




Volumn 85, Issue 1, 2010, Pages 11-18

Expression of intein-tagged fusion protein and its applications in downstream processing

Author keywords

Affinity tag; Intein; Intervening proteins; Protein purification; Protein splicing element; Self cleaving proteins

Indexed keywords

AFFINITY TAG; CONVENTIONAL METHODS; DOWNSTREAM-PROCESSING; EXPRESSION SYSTEM; FURTHER DEVELOPMENT; FUSION PROTEINS; INDUSTRIAL-SCALE PRODUCTION; INTEIN; PROTEIN PURIFICATION; PROTEIN-SPLICING; PURIFICATION PROCEDURES; PURIFICATION SYSTEMS; RECOMBINANT PROTEIN; TARGET PROTEINS;

EID: 75649127236     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.2277     Document Type: Short Survey
Times cited : (16)

References (59)
  • 1
    • 22444444258 scopus 로고    scopus 로고
    • Novel and economical purification of recombinant proteins: Intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
    • Banki MR, Gerngross TU and Wood DW, Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Sci 14:1387-1395 (2005).
    • (2005) Protein Sci , vol.14 , pp. 1387-1395
    • Banki, M.R.1    Gerngross, T.U.2    Wood, D.W.3
  • 2
    • 0035542874 scopus 로고    scopus 로고
    • Applications of novel affinity cassette methods: Use of peptide fusion handles for the purification of recombinant proteins
    • Hearn MT and Acosta D, Applications of novel affinity cassette methods: use of peptide fusion handles for the purification of recombinant proteins. J Mol Recognit 14:323-369 (2001).
    • (2001) J Mol Recognit , vol.14 , pp. 323-369
    • Hearn, M.T.1    Acosta, D.2
  • 3
    • 17144363589 scopus 로고    scopus 로고
    • Protein purification: Pure but not simple
    • Chapman T, Protein purification: pure but not simple. Nature 434:795-798 (2005).
    • (2005) Nature , vol.434 , pp. 795-798
    • Chapman, T.1
  • 4
    • 28144460981 scopus 로고    scopus 로고
    • Intein and affinity resins substitutes for protein purification and scale up
    • Banki MR and Wood DW, Intein and affinity resins substitutes for protein purification and scale up. Microb Cell Fact 4:1-6 (2005).
    • (2005) Microb Cell Fact , vol.4 , pp. 1-6
    • Banki, M.R.1    Wood, D.W.2
  • 5
    • 0029838842 scopus 로고    scopus 로고
    • The mechanism of protein splicing and its modulation by mutation
    • Xu MQ and Perler FB, The mechanism of protein splicing and its modulation by mutation. EMBO J 15:5146-5153 (1996).
    • (1996) EMBO J , vol.15 , pp. 5146-5153
    • Xu, M.Q.1    Perler, F.B.2
  • 6
    • 0028214350 scopus 로고
    • Protein splicing elements: Inteins and exteins - a definition of terms and recommended nomenclature
    • Perler FB, Davis EO, Dean GE, Gimble FS, Jack WE, Neff N, et al, Protein splicing elements: inteins and exteins - a definition of terms and recommended nomenclature. Nucleic Acids Res 22:1125-1127 (1994).
    • (1994) Nucleic Acids Res , vol.22 , pp. 1125-1127
    • Perler, F.B.1    Davis, E.O.2    Dean, G.E.3    Gimble, F.S.4    Jack, W.E.5    Neff, N.6
  • 7
    • 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, Mersha FB, Comb DG, Scott ME, Landry D, Vence LM, et al, Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 192:271-281 (1997).
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1    Mersha, F.B.2    Comb, D.G.3    Scott, M.E.4    Landry, D.5    Vence, L.M.6
  • 8
    • 0036915084 scopus 로고    scopus 로고
    • Intein-mediated affinity-fusion purification of the Escherichia coli RecA protein
    • Singleton SF, Simonette RA, Sharma NC and Roca AI, Intein-mediated affinity-fusion purification of the Escherichia coli RecA protein. Protein Expr Purif 26:476-488 (2002).
    • (2002) Protein Expr Purif , vol.26 , pp. 476-488
    • Singleton, S.F.1    Simonette, R.A.2    Sharma, N.C.3    Roca, A.I.4
  • 9
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self cleaving elastin-like polypeptide tags
    • Banki MR, Feng L and Wood DW, Simple bioseparations using self cleaving elastin-like polypeptide tags. Natural Methods 2:659-661 (2005).
    • (2005) Natural Methods , vol.2 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3
  • 10
    • 75649106570 scopus 로고    scopus 로고
    • IMPACT-CN System, New England Biolabs, Beverly, MA
    • IMPACT-CN System, Instructional manual #E6950S. New England Biolabs, Beverly, MA (2006).
    • (2006) Instructional manual , Issue.E6950S
  • 11
    • 75649101547 scopus 로고    scopus 로고
    • IMPACT-CN System, New England Biolabs, Beverly, MA
    • IMPACT-CN System, Instructional manual #E6901S. New England Biolabs, Beverly, MA (2007).
    • (2007) Instructional manual , Issue.E6901S
  • 12
    • 0025240361 scopus 로고
    • Molecular structure of a gene, VMA1, encoding the catalytic subunit of H+-translocating adenosine triphosphatase from vacuolar membranes of saccharomyces cerevisiae
    • Hirata R, Ohsumi Y, Nakano A, Kawasaki H, Suzuki K and Anraku Y, Molecular structure of a gene, VMA1, encoding the catalytic subunit of H+-translocating adenosine triphosphatase from vacuolar membranes of saccharomyces cerevisiae. J Biol Chem 265:6726-6733 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 6726-6733
    • Hirata, R.1    Ohsumi, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 13
    • 0025226104 scopus 로고
    • Protein splicing converts the yeast TFPI gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase
    • Kane PM, Yamashiro CT, Wolczyk DF, Neff N, Goebl M and Stevens TH, Protein splicing converts the yeast TFPI gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase. Science 250:651-657 (1990).
    • (1990) Science , vol.250 , pp. 651-657
    • Kane, P.M.1    Yamashiro, C.T.2    Wolczyk, D.F.3    Neff, N.4    Goebl, M.5    Stevens, T.H.6
  • 14
    • 4143058067 scopus 로고    scopus 로고
    • Synthetic two-piece and three-piece split inteins for protein trans-splicing
    • Sun WC, Yang J and Liu XQ, Synthetic two-piece and three-piece split inteins for protein trans-splicing. J Biol Chem 279:35281-35286 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 35281-35286
    • Sun, W.C.1    Yang, J.2    Liu, X.Q.3
  • 15
    • 0027373712 scopus 로고
    • Protein splicing: Selfish genes invade cellular proteins
    • Neff NF, Protein splicing: selfish genes invade cellular proteins. Curr Opin Cell Biol 5:971-976 (1993).
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 971-976
    • Neff, N.F.1
  • 16
    • 33751233858 scopus 로고    scopus 로고
    • Inteins, introns, and homing endonucleases: Recent revelations about the life cycle of parasitic genetic elements
    • Gogarten JPandHilario E, Inteins, introns, and homing endonucleases: recent revelations about the life cycle of parasitic genetic elements. BMC Evol Biol 6:1-5 (2006).
    • (2006) BMC Evol Biol , vol.6 , pp. 1-5
    • Gogarten JPandHilario, E.1
  • 17
    • 0032579457 scopus 로고    scopus 로고
    • Molecular dissection of the Mycobacterium tuberculosis RecA intein: Design of a minimal intein and of a trans-splicing system involving two intein fragments
    • Shinqledecker K, Jiang SQ and Paulus H, Molecular dissection of the Mycobacterium tuberculosis RecA intein: design of a minimal intein and of a trans-splicing system involving two intein fragments. Gene 207:187-195 (1998).
    • (1998) Gene , vol.207 , pp. 187-195
    • Shinqledecker, K.1    Jiang, S.Q.2    Paulus, H.3
  • 18
    • 25444447991 scopus 로고    scopus 로고
    • Cyclic peptides, a chemical genetics tool for biologists
    • Horswill AR and Benkovic SJ, Cyclic peptides, a chemical genetics tool for biologists. Cell Cycle 4:552-555 (2005).
    • (2005) Cell Cycle , vol.4 , pp. 552-555
    • Horswill, A.R.1    Benkovic, S.J.2
  • 19
    • 0033894562 scopus 로고    scopus 로고
    • Protein splicing and its application
    • Perler FB and Adam E, Protein splicing and its application. Curr Opin Biotechnol 11:377-383 (2000).
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 377-383
    • Perler, F.B.1    Adam, E.2
  • 20
    • 25144483825 scopus 로고    scopus 로고
    • Protein splicing: Its discovery and structural insight into novel chemical mechanisms
    • Anraku Y, Mizutani R and Satow Y, Protein splicing: its discovery and structural insight into novel chemical mechanisms. IUBMB Life 57:563-574 (2005).
    • (2005) IUBMB Life , vol.57 , pp. 563-574
    • Anraku, Y.1    Mizutani, R.2    Satow, Y.3
  • 21
    • 33748551323 scopus 로고    scopus 로고
    • Protein splicing in Cis and in Trans
    • Saleh L and Perler FB, Protein splicing in Cis and in Trans. Chem Record 6:183-193 (2006).
    • (2006) Chem Record , vol.6 , pp. 183-193
    • Saleh, L.1    Perler, F.B.2
  • 22
    • 23444433268 scopus 로고    scopus 로고
    • Protein splicing mechanisms and applications
    • Perler FB, Protein splicing mechanisms and applications. IUBMB Life 57:469-476 (2005).
    • (2005) IUBMB Life , vol.57 , pp. 469-476
    • Perler, F.B.1
  • 23
    • 0034665054 scopus 로고    scopus 로고
    • An alternative protein splicing mechanism for inteins lacking an N-terminal nucleophile
    • Southworth MW, Benner J and Perler FB, An alternative protein splicing mechanism for inteins lacking an N-terminal nucleophile. EMBO J 19:5019-5026 (2000).
    • (2000) EMBO J , vol.19 , pp. 5019-5026
    • Southworth, M.W.1    Benner, J.2    Perler, F.B.3
  • 24
    • 2442718804 scopus 로고    scopus 로고
    • Protein splicing of a Pyrococcus abyssi intein with a C-terminal glutamine
    • Mills KV, Manning JS, Garcia AM and Wuerdeman LA, Protein splicing of a Pyrococcus abyssi intein with a C-terminal glutamine. J Biol Chem 279:20685-20691 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 20685-20691
    • Mills, K.V.1    Manning, J.S.2    Garcia, A.M.3    Wuerdeman, L.A.4
  • 25
    • 0141755113 scopus 로고    scopus 로고
    • Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing
    • Ding Y, Xu MQ, Ghosh I, Chen X, Ferrandon S, Lesage G, et al, Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing. J Biol Chem 278:39133-39142 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 39133-39142
    • Ding, Y.1    Xu, M.Q.2    Ghosh, I.3    Chen, X.4    Ferrandon, S.5    Lesage, G.6
  • 26
    • 0034617214 scopus 로고    scopus 로고
    • Protein splicing in the absence of an intein penultimate histidine
    • Chen L, Benner J and Perler FB, Protein splicing in the absence of an intein penultimate histidine. J Biol Chem 275:20431-20435 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 20431-20435
    • Chen, L.1    Benner, J.2    Perler, F.B.3
  • 27
    • 0031938897 scopus 로고    scopus 로고
    • Modular organization of inteins and C-terminal autocatalytic domains
    • Pietrokovski S, Modular organization of inteins and C-terminal autocatalytic domains. Protein Sci 7:64-71 (1998).
    • (1998) Protein Sci , vol.7 , pp. 64-71
    • Pietrokovski, S.1
  • 28
    • 23444457741 scopus 로고    scopus 로고
    • Recent advances in protein splicing: Manipulating proteins in vitro and in vivo
    • Xu MQ and Evans TC Jr, Recent advances in protein splicing: manipulating proteins in vitro and in vivo. Curr Opin Biotechnol 16:440-446 (2005).
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 440-446
    • Xu, M.Q.1    Evans Jr, T.C.2
  • 29
    • 20444413435 scopus 로고    scopus 로고
    • Protein splicing elements and plants: From transgene containment to protein purification
    • Evans TC Jr, Xu MQ and Pradhan S, Protein splicing elements and plants: from transgene containment to protein purification. Annu Rev Plant Biol 56:375-392 (2005).
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 375-392
    • Evans Jr, T.C.1    Xu, M.Q.2    Pradhan, S.3
  • 30
    • 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 60:523-533 (2003).
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 31
    • 0023806075 scopus 로고    scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB and Johnson KS, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40 (1998).
    • (1998) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 32
    • 33646810065 scopus 로고    scopus 로고
    • Expression of N-terminal Cys-protein fragments using an intein refolding strategy
    • Hackenberger CP, Chen MM and Imperiali B, Expression of N-terminal Cys-protein fragments using an intein refolding strategy. Bioorgan Med Chem 14:5043-5048 (2006).
    • (2006) Bioorgan Med Chem , vol.14 , pp. 5043-5048
    • Hackenberger, C.P.1    Chen, M.M.2    Imperiali, B.3
  • 33
    • 57849151616 scopus 로고    scopus 로고
    • Intein-mediated rapid purification of recombinant maxadilan and M65 and their acute effects on plasma glucose
    • Yu R, Yi T, Zhang L, Hong A, Dai Y and Zhou T, Intein-mediated rapid purification of recombinant maxadilan and M65 and their acute effects on plasma glucose. Acta Biochim Biophys Sin 40:1015-1022 (2008).
    • (2008) Acta Biochim Biophys Sin , vol.40 , pp. 1015-1022
    • Yu, R.1    Yi, T.2    Zhang, L.3    Hong, A.4    Dai, Y.5    Zhou, T.6
  • 34
    • 44349158280 scopus 로고    scopus 로고
    • Simple protein purification through affinity adsorption on regenerated amorphous cellulose followed by intein self-cleavage
    • Hong J, Wang Y, Ye X and Zhang YH, Simple protein purification through affinity adsorption on regenerated amorphous cellulose followed by intein self-cleavage. J Chromatogr A 1194:150-154 (2008).
    • (2008) J Chromatogr A , vol.1194 , pp. 150-154
    • Hong, J.1    Wang, Y.2    Ye, X.3    Zhang, Y.H.4
  • 35
    • 33646778457 scopus 로고    scopus 로고
    • Intein-mediated rapid purification and characterization of a novel recombinant agonist for VPAC2
    • Yu RJ, Xie QL, Dai Y, Gao Y, Zhou TH and Hong A, Intein-mediated rapid purification and characterization of a novel recombinant agonist for VPAC2. Peptides 27:1359-1366 (2006).
    • (2006) Peptides , vol.27 , pp. 1359-1366
    • Yu, R.J.1    Xie, Q.L.2    Dai, Y.3    Gao, Y.4    Zhou, T.H.5    Hong, A.6
  • 36
    • 4444274531 scopus 로고    scopus 로고
    • Inteinmediated fusion expression, high efficient refolding, and one-step purification of gelonin toxin
    • Guo CY, Li ZY, Shi YW, Xu MQ, Wise JG, Trommer WE et al, Inteinmediated fusion expression, high efficient refolding, and one-step purification of gelonin toxin. Protein Expr Purif 37:361-367 (2004).
    • (2004) Protein Expr Purif , vol.37 , pp. 361-367
    • Guo, C.Y.1    Li, Z.Y.2    Shi, Y.W.3    Xu, M.Q.4    Wise, J.G.5    Trommer, W.E.6
  • 37
    • 15444373827 scopus 로고    scopus 로고
    • Intein-mediated rapid purification of recombinant human pituitary adenylate cyclase activating polypeptide
    • Yu RJ, Hong A, Dai Y and Gao Y, Intein-mediated rapid purification of recombinant human pituitary adenylate cyclase activating polypeptide. Acta Biochim Biophys Sin 36:759-766 (2004).
    • (2004) Acta Biochim Biophys Sin , vol.36 , pp. 759-766
    • Yu, R.J.1    Hong, A.2    Dai, Y.3    Gao, Y.4
  • 38
    • 33947657289 scopus 로고    scopus 로고
    • A novel recombinant, VPAC2-selective agonist enhancing insulin release and glucose disposal
    • Yu RJ, Tam NI, Gao Y, Zeng ZH, Zhou TH and Hong A, A novel recombinant, VPAC2-selective agonist enhancing insulin release and glucose disposal. Acta Pharmacol Sin 28:526-533 (2007).
    • (2007) Acta Pharmacol Sin , vol.28 , pp. 526-533
    • Yu, R.J.1    Tam, N.I.2    Gao, Y.3    Zeng, Z.H.4    Zhou, T.H.5    Hong, A.6
  • 39
    • 23244448024 scopus 로고    scopus 로고
    • Use of Ssp dnaB derived mini-intein as a fusion partner for production of recombinant human brain natriuretic peptide in Escherichia coli
    • Sun ZY, Chen JY, Yao HW, Liu LL, Wang J, Zhang J et al, Use of Ssp dnaB derived mini-intein as a fusion partner for production of recombinant human brain natriuretic peptide in Escherichia coli. Protein Expr Purif 43:26-32 (2005).
    • (2005) Protein Expr Purif , vol.43 , pp. 26-32
    • Sun, Z.Y.1    Chen, J.Y.2    Yao, H.W.3    Liu, L.L.4    Wang, J.5    Zhang, J.6
  • 40
    • 65049091114 scopus 로고    scopus 로고
    • Srinivasa Babu K,Muthukumaran T, Antony A, Prem Singh Samuel SD, Balamurali M, Murugan V et al, Single step intein-mediated purification of hGMCSF expressed in salt-inducible E. coli. Biotechnol Lett 31:659-664 (2009).
    • Srinivasa Babu K,Muthukumaran T, Antony A, Prem Singh Samuel SD, Balamurali M, Murugan V et al, Single step intein-mediated purification of hGMCSF expressed in salt-inducible E. coli. Biotechnol Lett 31:659-664 (2009).
  • 41
    • 54049122125 scopus 로고    scopus 로고
    • Simultaneous refolding and purification of a recombinant lipase with an intein tag by affinity precipitation with chitosan
    • Singh PK and Gupta MN, Simultaneous refolding and purification of a recombinant lipase with an intein tag by affinity precipitation with chitosan. Biochim Biophys Acta 1784:1825-1829 (2008).
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1825-1829
    • Singh, P.K.1    Gupta, M.N.2
  • 43
    • 61749100890 scopus 로고    scopus 로고
    • Soluble expression and one-step purification of a neurotoxin Huwentoxin-I in Escherichia coli
    • Che N, Wang L, Gao Y and An C, Soluble expression and one-step purification of a neurotoxin Huwentoxin-I in Escherichia coli. Protein Expres Purif 65:154-159 (2009).
    • (2009) Protein Expres Purif , vol.65 , pp. 154-159
    • Che, N.1    Wang, L.2    Gao, Y.3    An, C.4
  • 44
    • 33845932569 scopus 로고    scopus 로고
    • One-step purification of insoluble hydantoinase overproduced in Escherichia coli
    • Chiang CJ, Chen CC, Chao YP and Jason TC, One-step purification of insoluble hydantoinase overproduced in Escherichia coli. Protein Express Purif 52:14-18 (2007).
    • (2007) Protein Express Purif , vol.52 , pp. 14-18
    • Chiang, C.J.1    Chen, C.C.2    Chao, Y.P.3    Jason, T.C.4
  • 45
    • 57749193469 scopus 로고    scopus 로고
    • Utilization of protein splicing for purification of the human growth hormone
    • Starokadomskyy PL, Okunev OV, Irodov DM and Kordium VA, Utilization of protein splicing for purification of the human growth hormone. Mol Biol 42:966-972 (2008).
    • (2008) Mol Biol , vol.42 , pp. 966-972
    • Starokadomskyy, P.L.1    Okunev, O.V.2    Irodov, D.M.3    Kordium, V.A.4
  • 46
    • 67349157562 scopus 로고    scopus 로고
    • Optimizationof ELP-intein mediated protein purification by salt substitution
    • Fong BA, Wua WY and Wood DW,Optimizationof ELP-intein mediated protein purification by salt substitution. Protein Expres Purif 66:198-202 (2009).
    • (2009) Protein Expres Purif , vol.66 , pp. 198-202
    • Fong, B.A.1    Wua, W.Y.2    Wood, D.W.3
  • 47
    • 54349103050 scopus 로고    scopus 로고
    • One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester
    • Bastings MMC, Baal IV, Meijer EW and Merkx M, One-step refolding and purification of disulfide-containing proteins with a C-terminal MESNA thioester. BMC Biotechnol 8-76 (2008).
    • (2008) BMC Biotechnol , vol.8-76
    • Bastings, M.M.C.1    Baal, I.V.2    Meijer, E.W.3    Merkx, M.4
  • 48
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastin-like polypeptide tags
    • Banki MR, Feng L and Wood DW, Simple bioseparations using self-cleaving elastin-like polypeptide tags. Natural Methods 2:659-661 (2005).
    • (2005) Natural Methods , vol.2 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3
  • 50
    • 11844292771 scopus 로고    scopus 로고
    • High level expression and single-step purification of hexahistidine-tagged l-2- hydroxyisocaproate dehydrogenase making use of a versatile expression vector set
    • Chatterjee S, Schoepe J, Lohmer S and Schomburg D, High level expression and single-step purification of hexahistidine-tagged l-2- hydroxyisocaproate dehydrogenase making use of a versatile expression vector set. Protein Expr Purif 39:137-143 (2005).
    • (2005) Protein Expr Purif , vol.39 , pp. 137-143
    • Chatterjee, S.1    Schoepe, J.2    Lohmer, S.3    Schomburg, D.4
  • 51
    • 0023806075 scopus 로고    scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB and Johnson KS, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40 (1998).
    • (1998) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 52
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard BL, Chubet RG and Vizard DL, Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. Biotechniques 16:730-735 (1994).
    • (1994) Biotechniques , vol.16 , pp. 730-735
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 53
    • 0035975859 scopus 로고    scopus 로고
    • The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins
    • Einhauer A and Jungbauer A, The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins. J BiochemBiophys Methods 49:455-465 (2001).
    • (2001) J BiochemBiophys Methods , vol.49 , pp. 455-465
    • Einhauer, A.1    Jungbauer, A.2
  • 54
    • 0029865819 scopus 로고    scopus 로고
    • Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin
    • Schmidt TG, Koepke J, Frank R and Skerra A, Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin. JMol Biol 255:753-766 (1996).
    • (1996) JMol Biol , vol.255 , pp. 753-766
    • Schmidt, T.G.1    Koepke, J.2    Frank, R.3    Skerra, A.4
  • 55
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins
    • Skerra A and Schmidt TG, Use of the Strep-tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol 326:271-304 (2000).
    • (2000) Methods Enzymol , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.2
  • 56
    • 0020347668 scopus 로고
    • Maltose-binding protein from Escherichia coli
    • Kellerman OK and Ferenci T, Maltose-binding protein from Escherichia coli. Methods Enzymol 90:459-463 (1982).
    • (1982) Methods Enzymol , vol.90 , pp. 459-463
    • Kellerman, O.K.1    Ferenci, T.2
  • 57
    • 0038796540 scopus 로고    scopus 로고
    • Study of protein splicing and intein-mediated peptide bond cleavage under high-cell-density conditions
    • Sharma SS, Zhang A, Wang H, Harcum SW and Chong S, Study of protein splicing and intein-mediated peptide bond cleavage under high-cell-density conditions. Biotechnol Prog 19:1085-1090 (2003).
    • (2003) Biotechnol Prog , vol.19 , pp. 1085-1090
    • Sharma, S.S.1    Zhang, A.2    Wang, H.3    Harcum, S.W.4    Chong, S.5
  • 58
    • 33745991799 scopus 로고    scopus 로고
    • Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli
    • Sharma SS, Chong S and Harcum SW, Intein-mediated protein purification of fusion proteins expressed under high-cell density conditions in E. coli. J Biotechnol 125:48-56 (2006).
    • (2006) J Biotechnol , vol.125 , pp. 48-56
    • Sharma, S.S.1    Chong, S.2    Harcum, S.W.3
  • 59
    • 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 SS, Chong S and Harcum SW, Simulation of large-scale production of a soluble recombinant protein expressed in Escherichia coli using an intein-mediated purification system. Appl Biochem Biotechnol 126:93-118 (2005).
    • (2005) Appl Biochem Biotechnol , vol.126 , pp. 93-118
    • Sharma, S.S.1    Chong, S.2    Harcum, S.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.