综述 |
|
|
|
|
功能性包涵体的研究进展 |
罗莉1, 何勇智2, 张勇侠2, 王明蓉2 |
1. 中国医药集团总公司四川抗菌素工业研究所 成都 610052; 2. 成都生物制品研究所有限责任公司 成都 610023 |
|
Advances in the Study of non-classical Inclusion Bodies |
LUO Li1, HE Yong-zhi2, ZHANG Yong-xia2, WANG Ming-rong2 |
1. Sichuan Industrial Institute of Antibiotics, China National Pharmaceutical Corp., Chengdu 610052, China; 2. Chengdu Institute of Biological Products Co., Ltd., Chengdu 610023, China |
引用本文:
罗莉, 何勇智, 张勇侠, 王明蓉. 功能性包涵体的研究进展[J]. 中国生物工程杂志, 2013, 33(1): 114-121.
LUO Li, HE Yong-zhi, ZHANG Yong-xia, WANG Ming-rong. Advances in the Study of non-classical Inclusion Bodies. China Biotechnology, 2013, 33(1): 114-121.
链接本文:
https://manu60.magtech.com.cn/biotech/CN/
或
https://manu60.magtech.com.cn/biotech/CN/Y2013/V33/I1/114
|
[1] Jevševar S, Gaberc-Porekar V, Fonda I,et al.Production of nonclassical inclusion bodies from which correctly folded protein can be extracted.Biotechnol Progr, 2005, 21(2): 632-639.
[2] García-Fruitós E, González-Montalbán N, Morell M,et al.Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins.MicrobvCell Fact, 2005, 4(1): 27-32.
[3] Umetsu M, Tsumoto K, Nittaa S,et al.Nondenaturing solubilization of beta2 microglobulin from inclusion bodies by L-arginine.Biochem Bioph Res Co, 2005, 328(1): 189-197.
[4] Peternel Š, Bele M, Gaberc-Porekar V,et al.Nonclassical inclusion bodies in Escherichia coli.Microb Cell Fact, 2006, 5: 23-24.
[5] García-Fruitós E, Arís A, Villaverde A.Localization of functional polypeptides in bacterial inclusion bodies.Appl Environ Microb, 2007, 73(1): 289-294.
[6] Peternel Š, Grdadolnik J, Gaberc-Porekar V,et al.Engineering inclusion bodies for non denaturing extraction of functional proteins.Microb Cell Fact 2008, 7(1): 34-42.
[7] DM W, NH G.The formation of biologically active beta-galactosidase inclusion bodies in Escherichia coli.Australian Journal of Biotechnology, 1989, 3(1): 28-32.
[8] Tokatlidis K, Dhurjati P, Millet J,et al.High activity of inclusion bodies formed in Ecoli overproducing Clostridium thermocellum endoglucanase D.Febs Lett, 1991, 282(1): 205-208.
[9] González-Montalbán N, García-Fruitós E, Villaverde A.Recombinant protein solubility——does more mean better?.Nat Biotechnol, 2007, 25(7): 718-720.
[10] Kopito R R.Aggresomes,inclusion bodies and protein aggregation.Trends Cell Biol, 2000, 10(12): 524-530.
[11] Peternel Š, Komel R.Active protein aggregates produced in Escherichia coli. Int.J.Mol.Sci, 2011, 12(11): 8275-8287.
[12] García-Fruitós E, Vazquez E, Diez-Gil C,et al.Bacterial inclusion bodies:making gold from waste.Cell Press, 2012, 30(2): 65-70.
[13] Peternel Š, Bele M, Gaberc-Porekar V,et al.Inclusion bodies contraction with implications in biotechnology.Acta Chim Slov, 2008: 608-612.
[14] A JFK, Hartley DL.Formation of recombinant protein inclusion bodies in Escherichia coli.Trends Biotechnol, 1988, 6(5): 95-101.
[15] Vera A, N NGL, S AA,et al.The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures.Biotechnol Bioeng, 2007, 96(6): 1101-1106.
[16] Peternel Š, Gaberc-Porekar V, Komel R.Bacterial growth conditions affect quality of GFP expressed inside inclusion bodies.Acta Chim Slov, 2009, 56: 860-867.
[17] Sans C, Garcia-Fruitos E, Ferraz RM,et al.Inclusion bodies of fuculose-1-phosphate aldolase as stable and reusable biocatalysts.Biotechnol Progr, 2012, 28(2): 421-427.
[18] Rodríguez-Carmona E, Cano-Garrido O, Seras-Franzoso J,et al.Isolation of cell-free bacterial inclusion bodies.Microb Cell Fact, 2010, 9(1): 71-79.
[19] Arié J, Miot M, Sassoon N,et al.Formation of active inclusion bodies in the periplasm of Escherichia coli.Mol Microbiol, 2006, 62(2): 427-437.
[20] Wu W, Xing L, Zhou B,et al.Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli.Microb Cell Fact, 2011, 10(1): 9-16.
[21] Zhou B, Xing L, Wu W,et al.Small surfactant-like peptide can drive soluble proteins into active aggregates.Microb Cell Fact 2012, 11(1): 10-17.
[22] Nahalka J, Nidetzky B.Fusion to a pull-down domain: a novel approach of producing Trigonopsis variabilis D-amino acid oxidase as insoluble enzyme aggregates.Biotechnol Bioeng, 2007, 97(3): 454-461.
[23] Nahalka J.Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose-1-phosphate.J Ind Microbiol Biotechnol, 2008, 35(4): 219-223.
[24] Nahalka J, Vikartovska A, Hrabarova E.A crosslinked inclusion body process for sialic acid synthesis.J Biotechnol, 2008, 134(1-2): 146-153.
[25] Peternel Š, Komel R.Isolation of biologically active nanomaterial(inclusion bodies) from bacterial cells.Microb Cell Fact, 2010, 9(1): 66-81.
[26] Peternel S.Bacterial cell disruption: a crucial step in protein production.New Biotechnology, 2011, 00(00): xx-xx.
[27] Tsumoto K, Umetsu M, Kumagai I,et al.Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine.Biochem Biophys Res Commun, 2003, 312(4): 1383-1386.
[28] Oberg K, Chrunyk BA, Wetzel R,et al.Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR.Biochemistry-Us, 1994, 33(9): 2628-2634.
[29] Fine M, Amuly R, Sandowski Y,et al.Recombinant gilthead seabream (Sparus aurata) insulin-like growth factor-I: subcloning, expression in Escherichia coli, purification and characterization.J Endocrinol, 1997, 153(1): 139-150.
[30] Paduel A, Chapnik-Cohen N, Gertler A,et al.Preparation and Characterization of Recombinant Dolphin Fish(Coryphaena hippurus) Growth Hormone.Protein Expres Purif, 1999, 16(3): 417-423.
[31] Carrio M M, Cubarsib R, Villaverde A.Fine architecture of bacterial inclusion bodies.Febs Lett, 2000, 471(1): 7-11.
[32] Kuczynska-Wisnik D, Zurawa-Janicka D, Narkiewicz J,et al.Escherichia coli small heat shock proteins IbpA/B enhance activity of enzymes sequestered in inclusion bodies.Acta Biochim Pol, 2004, 51(4): 925-931.
[33] Ami D, Natalello A, Gatti-Lafranconi P,et al.Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy.Febs Lett, 2005, 579(16): 3433-3436.
[34] Solomon G, Niv-Spector L, Gonen-Berger D,et al.Preparation of leptin antagonists by site-directed mutagenesis of human,ovine,rat,and mouse leptin's site III.Ann Ny Acad Sci, 2006, 1091: 531-539.
[35] Nahalka J, Gemeiner P, Bucko M,et al.Bioenergy beads:a tool for regeneration of ATP/NTP in biocatalytic synthesis.Artif Cells Blood Substit and Biotechnol, 2006, 34(5): 515-521.
[36] Peternel Š, Jevševar S, Bele M,et al.New properties of inclusion bodies with implications for biotechnology.Biotechnol Appl Biochem, 2008, 49(Pt 4): 239-246.
[37] Tsuji I, Mastui H, Ito T,et al.L-cysteine-enhanced renaturation of bioactive soluble tumor necrosis factor ligand family member LIGHT from inclusion bodies in Escherichia coli.Protein Expres Purif, 2011, 80(2): 239-245.
[38] Carvajal P, Gibert J, Campos N,et al.Activity of maize transglutaminase overexpressed in Escherichia coli inclusion bodies:an alternative to protein refolding.Biotechnol Progr, 2011, 27(1): 232-240.
[39] Li M, Fan H, Liu J H,et al.High pH solubilization and chromatography-based renaturation and purification of recombinant human granulocyte colony-stimulating factor from inclusion bodies.Appl Biochem Biotech, 2012, 166(5): 1264-1274.
[40] Lu S C, Lin S C.Recovery of active N-acetyl-d-glucosamine 2-epimerase from inclusion bodies by solubilization with non-denaturing buffers.Enzyme Microb Tech, 2012, 50(1): 65-70.
[41] Liovic M, Ozir M, Zavec A B,et al.Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells.Microb Cell Fact, 2012, 11: 67-80.
[42] Singh S M, Sharma A, Upadhyay A K,et al.Solubilization of inclusion body proteins using n-propanol and its refolding into bioactive form.Protein Expres Purif, 2012, 81(1): 75-82.
[43] Walsh D J, Noble G P, Piro J R,et al.Non-reducing alkaline solubilization and rapid on-column refolding of recombinant prion protein.Prep Biochem and Biotechnol, 2012, 42(1): 77-86.
[44] Francis V G, Majeed M A, Gummadi S N.Recovery of functionally active recombinant human phospholipid scramblase 1 from inclusion bodies using N-lauroyl sarcosine.J Ind Microbiol Biotechnol, 2012, 39(7): 1041-1048.
[45] Nahalka J, Dib I, Nidetzky B.Encapsulation of Trigonopsis variabilis D-amino acid oxidase and fast comparison of the operational stabilities of free and immobilized preparations of the enzyme.Biotechnol Bioeng, 2008, 99(2): 251-260. |
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
|
Shared |
|
|
|
|
|
Discussed |
|
|
|
|