메뉴 건너뛰기




Volumn 588, Issue 2, 2014, Pages 247-252

Targeted expression, purification, and cleavage of fusion proteins from inclusion bodies in Escherichia coli

Author keywords

Chemical cleavage; Fusion protein; Inclusion body

Indexed keywords

2 (2 NITROPHENYL) 3 METHYL 3 BROMOINDOLENINE; 2 NITRO 5 THIOCYANATOBENZOIC ACID; ASPARAGINE; ASPARTIC ACID; BENZOIC ACID; BIOTIN; CHEMICAL COMPOUND; CYANOGEN BROMIDE; CYSTEINE; GLUTAMIC ACID; GLUTAMINE; GUANIDINE; HISTIDINE; HYBRID PROTEIN; METAL ION; METHIONINE; PAGP STEROID DELTA ISOMERASE; PALLADIUM; PURF STEROID DELTA ISOMERASE; STEROID DELTA ISOMERASE; STREPTAVIDIN; TRPLE STEROID DELTA ISOMERASE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; UREA;

EID: 84892370557     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.09.028     Document Type: Review
Times cited : (87)

References (58)
  • 1
    • 0023050642 scopus 로고
    • The purification of eukaryotic polypeptides synthesized in Escherichia coli
    • F.A. Marston The purification of eukaryotic polypeptides synthesized in Escherichia coli Biochem. J. 240 1986 1 12
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.1
  • 2
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 0033386134 scopus 로고    scopus 로고
    • Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies
    • S. Misawa, and I. Kumagai Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies Biopolymers 51 1999 297 307
    • (1999) Biopolymers , vol.51 , pp. 297-307
    • Misawa, S.1    Kumagai, I.2
  • 6
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: Biological role of inclusion bodies
    • A. Villaverde, and M.M. Carrio Protein aggregation in recombinant bacteria: biological role of inclusion bodies Biotechnol. Lett. 25 2003 1385 1395
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Carrio, M.M.2
  • 7
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • A.M. Fernandez-Escamilla, F. Rousseau, J. Schymkowitz, and L. Serrano Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat. Biotechnol. 22 2004 1302 1306
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 8
    • 0017873186 scopus 로고
    • Translation of the leader region of the Escherichia coli tryptophan operon
    • G.F. Miozzari, and C. Yanofsky Translation of the leader region of the Escherichia coli tryptophan operon J. Bacteriol. 133 1978 1457 1466
    • (1978) J. Bacteriol. , vol.133 , pp. 1457-1466
    • Miozzari, G.F.1    Yanofsky, C.2
  • 9
    • 0021752924 scopus 로고
    • Human transforming growth factor-alpha: Precursor structure and expression in E. Coli
    • R. Derynck, A.B. Roberts, M.E. Winkler, E.Y. Chen, and D.V. Goeddel Human transforming growth factor-alpha: precursor structure and expression in E. Coli Cell 38 1984 287 297
    • (1984) Cell , vol.38 , pp. 287-297
    • Derynck, R.1    Roberts, A.B.2    Winkler, M.E.3    Chen, E.Y.4    Goeddel, D.V.5
  • 10
    • 79954972264 scopus 로고    scopus 로고
    • Expression and purification of the membrane protein p7 from hepatitis C virus
    • G.A. Cook, S. Stefer, and S.J. Opella Expression and purification of the membrane protein p7 from hepatitis C virus Biopolymers 96 2011 32 40
    • (2011) Biopolymers , vol.96 , pp. 32-40
    • Cook, G.A.1    Stefer, S.2    Opella, S.J.3
  • 11
    • 0028017482 scopus 로고
    • Production, purification, and cleavage of tandem repeats of recombinant peptides
    • A. Kuliopulos, and C.T. Walsh Production, purification, and cleavage of tandem repeats of recombinant peptides J. Am. Chem. Soc. 116 1994 4599 4607
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4599-4607
    • Kuliopulos, A.1    Walsh, C.T.2
  • 12
    • 80054062747 scopus 로고    scopus 로고
    • Recombinant production of antimicrobial peptides in Escherichia coli: A review
    • Y. Li Recombinant production of antimicrobial peptides in Escherichia coli: a review Protein Expr. Purif. 80 2011 260 267
    • (2011) Protein Expr. Purif. , vol.80 , pp. 260-267
    • Li, Y.1
  • 13
    • 0034597709 scopus 로고    scopus 로고
    • High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies
    • J.H. Lee, J.H. Kim, S.W. Hwang, W.J. Lee, H.K. Yoon, H.S. Lee, and S.S. Hong High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies Biochem. Biophys. Res. Commun. 277 2000 575 580
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 575-580
    • Lee, J.H.1    Kim, J.H.2    Hwang, S.W.3    Lee, W.J.4    Yoon, H.K.5    Lee, H.S.6    Hong, S.S.7
  • 15
    • 65349123502 scopus 로고    scopus 로고
    • Production and isotope labeling of antimicrobial peptides in Escherichia coli by means of a novel fusion partner that enables high-yield insoluble expression and fast purification
    • V. Vidovic, L. Prongidi-Fix, B. Bechinger, and S. Werten Production and isotope labeling of antimicrobial peptides in Escherichia coli by means of a novel fusion partner that enables high-yield insoluble expression and fast purification J. Pept. Sci. 15 2009 278 284
    • (2009) J. Pept. Sci. , vol.15 , pp. 278-284
    • Vidovic, V.1    Prongidi-Fix, L.2    Bechinger, B.3    Werten, S.4
  • 17
    • 84864943653 scopus 로고    scopus 로고
    • A PagP fusion protein system for the expression of intrinsically disordered proteins in Escherichia coli
    • P.M. Hwang, J.S. Pan, and B.D. Sykes A PagP fusion protein system for the expression of intrinsically disordered proteins in Escherichia coli Protein Expr. Purif. 85 2012 148 151
    • (2012) Protein Expr. Purif. , vol.85 , pp. 148-151
    • Hwang, P.M.1    Pan, J.S.2    Sykes, B.D.3
  • 19
  • 20
    • 0038395927 scopus 로고    scopus 로고
    • The solvent in CNBr cleavage reactions determines the fragmentation efficiency of ketosteroid isomerase fusion proteins used in the production of recombinant peptides
    • J.C. Rodriguez, L. Wong, and P.A. Jennings The solvent in CNBr cleavage reactions determines the fragmentation efficiency of ketosteroid isomerase fusion proteins used in the production of recombinant peptides Protein Expr. Purif. 28 2003 224 231
    • (2003) Protein Expr. Purif. , vol.28 , pp. 224-231
    • Rodriguez, J.C.1    Wong, L.2    Jennings, P.A.3
  • 22
    • 0030669141 scopus 로고    scopus 로고
    • A novel procedure for the efficient purification of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • M. Ramjeesingh, C. Li, E. Garami, L.J. Huan, M. Hewryk, Y. Wang, K. Galley, and C.E. Bear A novel procedure for the efficient purification of the cystic fibrosis transmembrane conductance regulator (CFTR) Biochem. J. 327 1997 17 21
    • (1997) Biochem. J. , vol.327 , pp. 17-21
    • Ramjeesingh, M.1    Li, C.2    Garami, E.3    Huan, L.J.4    Hewryk, M.5    Wang, Y.6    Galley, K.7    Bear, C.E.8
  • 23
    • 77049094645 scopus 로고    scopus 로고
    • Single-step affinity purification of recombinant proteins using the silica-binding Si-tag as a fusion partner
    • T. Ikeda, K. Ninomiya, R. Hirota, and A. Kuroda Single-step affinity purification of recombinant proteins using the silica-binding Si-tag as a fusion partner Protein Expr. Purif. 71 2010 91 95
    • (2010) Protein Expr. Purif. , vol.71 , pp. 91-95
    • Ikeda, T.1    Ninomiya, K.2    Hirota, R.3    Kuroda, A.4
  • 24
    • 79952627013 scopus 로고    scopus 로고
    • The silica-binding Si-tag functions as an affinity tag even under denaturing conditions
    • T. Ikeda, K. Motomura, Y. Agou, T. Ishida, R. Hirota, and A. Kuroda The silica-binding Si-tag functions as an affinity tag even under denaturing conditions Protein Expr. Purif. 77 2011 173 177
    • (2011) Protein Expr. Purif. , vol.77 , pp. 173-177
    • Ikeda, T.1    Motomura, K.2    Agou, Y.3    Ishida, T.4    Hirota, R.5    Kuroda, A.6
  • 25
    • 0034536389 scopus 로고    scopus 로고
    • Charge engineering of a protein domain to allow efficient ion-exchange recovery
    • T. Graslund, G. Lundin, M. Uhlen, P.A. Nygren, and S. Hober Charge engineering of a protein domain to allow efficient ion-exchange recovery Protein Eng. 13 2000 703 709
    • (2000) Protein Eng. , vol.13 , pp. 703-709
    • Graslund, T.1    Lundin, G.2    Uhlen, M.3    Nygren, P.A.4    Hober, S.5
  • 26
    • 33750601043 scopus 로고    scopus 로고
    • Single-step recovery and solid-phase refolding of inclusion body proteins using a polycationic purification tag
    • M. Hedhammar, T. Alm, T. Graslund, and S. Hober Single-step recovery and solid-phase refolding of inclusion body proteins using a polycationic purification tag Biotechnol. J. 1 2006 187 196
    • (2006) Biotechnol. J. , vol.1 , pp. 187-196
    • Hedhammar, M.1    Alm, T.2    Graslund, T.3    Hober, S.4
  • 27
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • D. Beckett, E. Kovaleva, and P.J. Schatz A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation Protein Sci. 8 1999 921 929
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 28
    • 0033819031 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo and in vitro using small peptide tags
    • M.G. Cull, and P.J. Schatz Biotinylation of proteins in vivo and in vitro using small peptide tags Methods Enzymol. 326 2000 430 440
    • (2000) Methods Enzymol. , vol.326 , pp. 430-440
    • Cull, M.G.1    Schatz, P.J.2
  • 29
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivocross-linking
    • C. Tagwerker, K. Flick, M. Cui, C. Guerrero, Y. Dou, B. Auer, P. Baldi, L. Huang, and P. Kaiser A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking Mol. Cell. Proteomics 5 2006 737 748
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 30
    • 0029865333 scopus 로고    scopus 로고
    • Correction for amino acid loss during acid hydrolysis of a purified protein
    • A.J. Darragh, D.J. Garrick, P.J. Moughan, and W.H. Hendriks Correction for amino acid loss during acid hydrolysis of a purified protein Anal. Biochem. 236 1996 199 207
    • (1996) Anal. Biochem. , vol.236 , pp. 199-207
    • Darragh, A.J.1    Garrick, D.J.2    Moughan, P.J.3    Hendriks, W.H.4
  • 31
    • 0025947262 scopus 로고
    • Development of an acid hydrolysis method with high recoveries of tryptophan and cysteine for microquantities of protein
    • H. Yamada, H. Moriya, and A. Tsugita Development of an acid hydrolysis method with high recoveries of tryptophan and cysteine for microquantities of protein Anal. Biochem. 198 1991 1 5
    • (1991) Anal. Biochem. , vol.198 , pp. 1-5
    • Yamada, H.1    Moriya, H.2    Tsugita, A.3
  • 32
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • R. Tyler-Cross, and V. Schirch Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides J. Biol. Chem. 266 1991 22549 22556
    • (1991) J. Biol. Chem. , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 33
    • 84866868392 scopus 로고    scopus 로고
    • A novel method for the large-scale production of PG-CNP37, a C-type natriuretic peptide analogue
    • S. Long, D.J. Wendt, S.M. Bell, T.W. Taylor, J.Y. Dewavrin, and M.C. Vellard A novel method for the large-scale production of PG-CNP37, a C-type natriuretic peptide analogue J. Biotechnol. 164 2012 196 201
    • (2012) J. Biotechnol. , vol.164 , pp. 196-201
    • Long, S.1    Wendt, D.J.2    Bell, S.M.3    Taylor, T.W.4    Dewavrin, J.Y.5    Vellard, M.C.6
  • 34
    • 0016550483 scopus 로고
    • Chemical and nutritional modifications of sunflower proteins due to alkaline processing. Formation of amino acid cross-links and isomerization of lysine residues
    • M.M. Provansal, J.L. Cuq, and J.C. Cheftel Chemical and nutritional modifications of sunflower proteins due to alkaline processing. Formation of amino acid cross-links and isomerization of lysine residues J. Agric. Food Chem. 23 1975 938 943
    • (1975) J. Agric. Food Chem. , vol.23 , pp. 938-943
    • Provansal, M.M.1    Cuq, J.L.2    Cheftel, J.C.3
  • 35
    • 0019887610 scopus 로고
    • Chemical cleavage of tryptophanyl and tyrosyl peptide bonds via oxidative halogenation mediated by o-iodosobenzoic acid
    • A. Fontana, D. Dalzoppo, C. Grandi, and M. Zambonin Chemical cleavage of tryptophanyl and tyrosyl peptide bonds via oxidative halogenation mediated by o-iodosobenzoic acid Biochemistry 20 1981 6997 7004
    • (1981) Biochemistry , vol.20 , pp. 6997-7004
    • Fontana, A.1    Dalzoppo, D.2    Grandi, C.3    Zambonin, M.4
  • 36
    • 0037067775 scopus 로고    scopus 로고
    • The reactivity and oxidation pathway of cysteine 232 in recombinant human alpha 1-antitrypsin
    • S.W. Griffiths, J. King, and C.L. Cooney The reactivity and oxidation pathway of cysteine 232 in recombinant human alpha 1-antitrypsin J. Biol. Chem. 277 2002 25486 25492
    • (2002) J. Biol. Chem. , vol.277 , pp. 25486-25492
    • Griffiths, S.W.1    King, J.2    Cooney, C.L.3
  • 37
    • 73049160443 scopus 로고
    • Non-enzymatic cleavage of peptide bonds: The methionine residues in bovine pancreatic ribonuclease
    • E. Gross, and B. Witkop Non-enzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease J. Biol. Chem. 237 1962 1856 1860
    • (1962) J. Biol. Chem. , vol.237 , pp. 1856-1860
    • Gross, E.1    Witkop, B.2
  • 38
    • 0014484242 scopus 로고
    • An examination of conditions for the cleavage of polypeptide chains with cyanogen bromide: Application to catalase
    • W.A. Schroeder, J.B. Shelton, and J.R. Shelton An examination of conditions for the cleavage of polypeptide chains with cyanogen bromide: application to catalase Arch. Biochem. Biophys. 130 1969 551 556
    • (1969) Arch. Biochem. Biophys. , vol.130 , pp. 551-556
    • Schroeder, W.A.1    Shelton, J.B.2    Shelton, J.R.3
  • 39
    • 0032953154 scopus 로고    scopus 로고
    • Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds
    • R. Kaiser, and L. Metzka Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds Anal. Biochem. 266 1999 1 8
    • (1999) Anal. Biochem. , vol.266 , pp. 1-8
    • Kaiser, R.1    Metzka, L.2
  • 40
    • 0020014653 scopus 로고
    • Oxidation of methionine to methionine sulfoxide as a side reaction of cyanogen bromide cleavage
    • R. Joppich-Kuhn, J.A. Corkill, and R.W. Giese Oxidation of methionine to methionine sulfoxide as a side reaction of cyanogen bromide cleavage Anal. Biochem. 119 1982 73 77
    • (1982) Anal. Biochem. , vol.119 , pp. 73-77
    • Joppich-Kuhn, R.1    Corkill, J.A.2    Giese, R.W.3
  • 41
    • 0035339118 scopus 로고    scopus 로고
    • Mass spectrometric analysis of cyanogen bromide fragments of integral membrane proteins at the picomole level: Application to rhodopsin
    • P. Kraft, J. Mills, and E. Dratz Mass spectrometric analysis of cyanogen bromide fragments of integral membrane proteins at the picomole level: application to rhodopsin Anal. Biochem. 292 2001 76 86
    • (2001) Anal. Biochem. , vol.292 , pp. 76-86
    • Kraft, P.1    Mills, J.2    Dratz, E.3
  • 42
    • 0015895285 scopus 로고
    • Specific chemical cleavage in high yield at the amino peptide bonds of cysteine and cystine residues
    • G.R. Jacobson, M.H. Schaffer, G.R. Stark, and T.C. Vanaman Specific chemical cleavage in high yield at the amino peptide bonds of cysteine and cystine residues J. Biol. Chem. 248 1973 6583 6591
    • (1973) J. Biol. Chem. , vol.248 , pp. 6583-6591
    • Jacobson, G.R.1    Schaffer, M.H.2    Stark, G.R.3    Vanaman, T.C.4
  • 43
    • 4644328635 scopus 로고    scopus 로고
    • Identification of alternative products and optimization of 2-nitro-5-thiocyanatobenzoic acid cyanylation and cleavage at cysteine residues
    • H.Y. Tang, and D.W. Speicher Identification of alternative products and optimization of 2-nitro-5-thiocyanatobenzoic acid cyanylation and cleavage at cysteine residues Anal. Biochem. 334 2004 48 61
    • (2004) Anal. Biochem. , vol.334 , pp. 48-61
    • Tang, H.Y.1    Speicher, D.W.2
  • 44
    • 0014940086 scopus 로고
    • Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations
    • D. Piszkiewicz, M. Landon, and E.L. Smith Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations Biochem. Biophys. Res. Commun. 40 1970 1173 1178
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1173-1178
    • Piszkiewicz, D.1    Landon, M.2    Smith, E.L.3
  • 45
    • 0014962696 scopus 로고
    • The specific non-enzymatic cleavage of bovine ribonuclease with hydroxylamine
    • P. Bornstein, and G. Balian The specific non-enzymatic cleavage of bovine ribonuclease with hydroxylamine J. Biol. Chem. 245 1970 4854 4856
    • (1970) J. Biol. Chem. , vol.245 , pp. 4854-4856
    • Bornstein, P.1    Balian, G.2
  • 46
    • 0030570130 scopus 로고    scopus 로고
    • Optimization of the hydroxylamine cleavage of an expressed fusion protein to produce recombinant human insulin-like growth factor (IGF)-I
    • S.J. Milner, S.M. Thomas, F.J. Ballard, and G.L. Francis Optimization of the hydroxylamine cleavage of an expressed fusion protein to produce recombinant human insulin-like growth factor (IGF)-I Biotechnol. Bioeng. 50 1996 265 272
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 265-272
    • Milner, S.J.1    Thomas, S.M.2    Ballard, F.J.3    Francis, G.L.4
  • 47
    • 53149094669 scopus 로고    scopus 로고
    • Chemical cleavage of bovine beta-lactoglobulin by BNPS-skatole for preparative purposes: Comparative study of hydrolytic procedures and peptide characterization
    • V. Rahali, and J. Gueguen Chemical cleavage of bovine beta-lactoglobulin by BNPS-skatole for preparative purposes: comparative study of hydrolytic procedures and peptide characterization J. Protein Chem. 18 1999 1 12
    • (1999) J. Protein Chem. , vol.18 , pp. 1-12
    • Rahali, V.1    Gueguen, J.2
  • 48
    • 0014961856 scopus 로고
    • Modification of the single tryptophan residue of staphylococcal nuclease by a new mild oxidizing agent
    • G.S. Omenn, A. Fontana, and C.B. Anfinsen Modification of the single tryptophan residue of staphylococcal nuclease by a new mild oxidizing agent J. Biol. Chem. 245 1970 1895 1902
    • (1970) J. Biol. Chem. , vol.245 , pp. 1895-1902
    • Omenn, G.S.1    Fontana, A.2    Anfinsen, C.B.3
  • 49
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • E.R. Stadtman Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions Annu. Rev. Biochem. 62 1993 797 821
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 54
    • 77949358922 scopus 로고    scopus 로고
    • Sequence-specific Ni(II)-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences
    • A. Krezel, E. Kopera, A.M. Protas, J. Poznanski, A. Wyslouch-Cieszynska, and W. Bal Sequence-specific Ni(II)-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences J. Am. Chem. Soc. 132 2010 3355 3366
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3355-3366
    • Krezel, A.1    Kopera, E.2    Protas, A.M.3    Poznanski, J.4    Wyslouch-Cieszynska, A.5    Bal, W.6
  • 55
    • 84860524464 scopus 로고    scopus 로고
    • Application of Ni(II)-assisted peptide bond hydrolysis to non-enzymatic affinity tag removal
    • E. Kopera, A. Belczyk-Ciesielska, and W. Bal Application of Ni(II)-assisted peptide bond hydrolysis to non-enzymatic affinity tag removal PLoS ONE 7 2012 e36350
    • (2012) PLoS ONE , vol.7 , pp. 36350
    • Kopera, E.1    Belczyk-Ciesielska, A.2    Bal, W.3
  • 56
    • 0037460193 scopus 로고    scopus 로고
    • Palladium(II) complex as a sequence-specific peptidase: Hydrolytic cleavage under mild conditions of X-Pro peptide bonds in X-Pro-Met and X-Pro-His segments
    • N.M. Milovic, and N.M. Kostic Palladium(II) complex as a sequence-specific peptidase: hydrolytic cleavage under mild conditions of X-Pro peptide bonds in X-Pro-Met and X-Pro-His segments J. Am. Chem. Soc. 125 2003 781 788
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 781-788
    • Milovic, N.M.1    Kostic, N.M.2
  • 57
    • 0038751861 scopus 로고    scopus 로고
    • An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs at the low pH of the late secretory pathway
    • M.E. Lidell, M.E. Johansson, and G.C. Hansson An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs at the low pH of the late secretory pathway J. Biol. Chem. 278 2003 13944 13951
    • (2003) J. Biol. Chem. , vol.278 , pp. 13944-13951
    • Lidell, M.E.1    Johansson, M.E.2    Hansson, G.C.3
  • 58
    • 0028066053 scopus 로고
    • Site-specific hydrolytic cleavage of cytochrome-c and of its heme undecapeptide, promoted by co-ordination complexes of palladium(II)
    • L.G. Zhu, L. Qin, T.N. Parac, and N.M. Kostic Site-specific hydrolytic cleavage of cytochrome-c and of its heme undecapeptide, promoted by co-ordination complexes of palladium(II) J. Am. Chem. Soc. 116 1994 5218 5224
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5218-5224
    • Zhu, L.G.1    Qin, L.2    Parac, T.N.3    Kostic, N.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.