Production of salmon calcitonin by direct expression of a glycine-extended precursor in Escherichia coli

Protein Expression and Purification

Volumn 26, Issue 2, 2002, Pages 249-259

  Ray, Martha V L ^a   Meenan, Christopher P ^a   Consalvo, Angelo P ^a   Smith, Carrie A ^a   Parton, Douglas P ^a   Sturmer, Amy M ^a   Shields, Paul P ^a   Mehta, Nozer M ^a  

^a Unigene Laboratories Incorporated   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

CALCITONIN; GLYCINE; PRIMER DNA; PROTEIN PRECURSOR; RECOMBINANT PROTEIN; SALCATONIN;

ARTICLE; BIOSYNTHESIS; CHEMISTRY; CULTURE MEDIUM; ESCHERICHIA COLI; FERMENTATION; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NUCLEOTIDE SEQUENCE;

BASE SEQUENCE; CALCITONIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CULTURE MEDIA, CONDITIONED; DNA PRIMERS; ESCHERICHIA COLI; FERMENTATION; GLYCINE; PROTEIN PRECURSORS; RECOMBINANT PROTEINS;

EID: 0036425101     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00523-5     Document Type: Article

References (39)

1. J.A. Stader, T.J. Silhavy, Engineering Escherichia coli to secrete heterologous gene products, in: David V. Goeddel (Ed.), Gene Expression Technology Methods in Enzymology, vol. 185, Academic Press Inc., San Diego, CA, 1990, pp. 166-187.
2. S. Josephson, R. Bishop, Secretion of peptides from E. coli: A production system for the pharmaceutical industry, Trends Biotechnol. 6 (1988) 218-224.
3. F. Baneyx, Recombinant protein expression in Escherichia coli, Curr. Opin. Biotechnol. 10 (1999) 411-421.
4. H. Nikaido, Outer membrane, in: F. Neidhardt (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, vol. 1, ASM Press, Washington, DC, 1996, pp. 29-47.
5. D. Atlan, J.C. Lazzaroni, R. Portalier, Effects of pho regulatory mutations and pho A amplification on alkaline phosphatase synthesis and release by lky mutants of Escherichia coli, J. Gen. Microbiol. 132 (Pt.1) (1986) 171-181.
6. H. Hsiung et al., Use of bacteriocin release protein in Escherichia coli for excretion of human growth hormone into the culture medium, Bio/Technol. 7 (1989) 267-271.
7. J. Robbens et al., Production of soluble and active recombinant murine interleukin-2 in Escherichia coli: High-level expression kil-induced release and purification, Protein Expr. Purif. 6 (1995) 481-486.
8. D. Koshland, D. Botstein, Secretion of β-lactamase requires the carboxyl end of the protein, Cell 20 (3) (1980) 749-760.
9. J. Blackwell, R. Horan, A novel strategy for production of a highly expressed recombinant protein in an active form, FEBS Lett. 295 (123) (1991) 10-12.
10. W.J. Quax, Merits of secretion of heterologous proteins by industrial microorganisms, Folia Microbiol. 42 (2) (1997) 99-103.
11. M.A. Molina, F. Aviles, E. Querol, Expression of a synthetic gene encoding potato carboxypeptidase inhibitor using a bacterial secretion vector, Gene 116 (1992) 129-138.
12. P. Slos et al., Recombinant cholera toxin B subunit in Escherichia coli: High level secretion, purification, and characterization, Protein Expr. Purif. 5 (1994) 518-526.
13. K.R. Oldenburg, A.L. D'Orfani, H.E. Selick, A method for the high level expression of a parathyroid hormone analog in E. coli, Protein Expr. Purif. 5 (1994) 278-284.
14. R.M. Belagaje, Increased production of low molecular weight recombinant proteins in Escherichia coli, Protein Sci. 6 (9) (1997) 1953-1962.
15. X.Q. Liu, S. Zhang, X.-M. Pan, C. Wang, A novel method for increasing production of mature protein in the periplasm of Escherichia coli, Protein Sci. 8 (1999) 2085-2089.
16. J. Winter, P. Neubauer, R. Glockshuber, R. Rudolph, Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA, J. Biotechnol. 84 (2) (2001) 175-185.
17. M. Rattenholl, Pro-sequence assisted folding and disulfide bond of human nerve growth factor, J. Mol. Biol. 305 (3) (2001) 523-533.
18. Y. Murakami et al., Construction of new excretion vectors: Two and three tandemly located promoters are active for extracellular protein production from Escherichia coli, Appl. Microbiol. Biotechnol. 30 (1989) 619-623.
19. D.M. Dykxhoorn, R. St. Pierre, T. Linn, A set of compatible tac promoter expression vectors, Gene 177 (1-2) (1996) 133-136.
20. J. Ghrayeb et al., Secretion cloning vectors in Escherichia coli, EMBO J. 3 (10) (1984) 2437-2442.
21. J. Perez-Perez, G. Marquez, J.L. Barbero, J. Guiterrez, Increasing the efficiency of protein export in E. coli, Bio/Technol. 12 (1994) 178-180.
22. J. Koke, M. Yang, D.J. Henner, J.J. Volwerk, O.H. Griffith, High-level expression in Escherichia coli and rapid purification of phosphatidylinositol-specific phospholipase C from Bacillus cereus and Bacillus thuringiensis, Protein Expr. Purif. 2 (1991) 51-58.
23. L. Ying, L. Shengdong, Tandem repeating of the expression cartridge - A novel strategy to enhance the expression efficiency of cloned gene in Escherichia coli, Chin. Med. Sci. J. 11 (1) (1996) 204-208.
24. R. Wetzel et al., Expression in Escherichia coli of a chemically synthesized gene for "mini-C" analog of human insulin, Gene 16 (1981) 63-71.
25. M.V.L. Ray et al., Production of recombinant salmon calcitonin by in vitro amidation of an Escherichia coli produced precursor peptide, Bio/Technol. 11 (1993) 64-70.
26. D.J. Korz, U. Rinas, K. Hellmuth, E.A. Sanders, W.D. Deckwer, Simple fed-batch technique for high cell density cultivation of Escherichia coli, J. Biotechnol. 39 (1995) 59-65.
27. S. Cabilly, Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments in Escherichia coli, Gene 85 (2) (1989) 553-557.
28. H. Takagi, Y. Morinaga, M. Tsushiya, H. Ikemura, M. Inouye, Control of folding of proteins secreted by a high expression secretion vector, pIN-III ompA: 16-Fold increase in production of active subtilisin E in Escherichia coli, Bio/Technol. 6 (1988) 948-950.
29. M. Tajima, T. Iida, T. Kaminuma, M. Yanagi, T. Fukushima, High-level synthesis in Escherichia coli of recombinant human calcitonin: Collagenase cleavage of the fusion protein and peptidylglycine α-amidation, J. Ferm. Bioeng. 72 (5) (1991) 362-367.
30. D. Hong, Z. Mingqiang, L. Min, C. Changqing, M. Jifang, Production of recombinant salmon calcitonin by amidation of precursor peptide using enzymatic transacylation and photolysis in vitro, Biochem. Biophys. Res. Commun. 267 (2000) 362-367.
31. S. Maclntyre, U. Henning, The role of the mature part of secretory proteins in translocation across the plasma membrane and in regulation of their synthesis in Escherichia coli, Biochimie 72 (1990) 157-167.
32. S.-Z. Pang et al., Expression of a gene encoding a scorpion insectotoxin peptide in yeast, bacteria, and plants, Gene 116 (1992) 165-172.
33. M. Better, C.P. Cheng, R. Robinson, A. Horwitz, Escherichia coli secretion of an active chimeric antibody fragment, Science 240 (1988) 1041-1043.
34. G. Georgiou, M.L. Shuler, D.B. Wilson, Release of periplasmic enzymes and other physiological effects of β-lactamase overproduction in Escherichia coli, Biotechnol. Bioeng. 32 (1988) 741-748.
35. F. Maywald et al., Human pancreatic secretory trypsin inhibitor PSTI produced in active form and secreted from Escherichia coli, Gene 68 (1988) 357-369.
36. B.R. Allen, G.W. Luli, A gradient-feed process for E. coli fermentations, BioPharm (November) (1987) 38-41.
37. D.J. Merkler, S.D. Young, Recombinant type A rat 75-kDa α-amidating enzyme catalyzes the conversion of glycine-extended peptides to peptide amides via an α-hydroxglycine intermediate, Arch. Biochem. Biophys. 289 (1) (1991) 192-196.
38. K.J. Watkins, Peptides: A boom in the making, C and E News. 8 (January) (2001) 11-15.
39. D.A. Miller et al., Characterization of a bifunctional peptidylglycine α-amidating enzyme expressed in Chinese Hamster Ovary cells, Arch. Biochem. Biophys. 298 (2) (1992) 380-388.