References
- Araujo AP, Oliva G, Henrique-Silva F, Garratt RC, Caceres O, Beltramini LM. 2000. Influence of the histidine tail on the structure and activity of recombinant chlorocatechol 1,2-dioxygenase. Biochem Biophys Res Commun. 272:480-484. https://doi.org/10.1006/bbrc.2000.2802
- Davis GD, Elisee C, Newham DM, Harrison RG. 1999. New fusion protein systems designed 289 to give soluble expression in Escherichia coli. Biotechnol Bioeng. 65:382-388. https://doi.org/10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.0.CO;2-I
- Engstrom A, Xanthopoulos KG, Boman HG, Bennich H. 1985. Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia. EMBO J. 4:2119-2122.
- Esposito D, Chatterjee DK. 2006. Enhancement of soluble protein expression through the use of fusion tags. Curr Opin Biotech. 17:353-358. https://doi.org/10.1016/j.copbio.2006.06.003
- Georgiou G, Valax P. 1996. Expression of correctly folded proteins in Escherichia coli. Curr Opin Biotech. 7:190-197. https://doi.org/10.1016/S0958-1669(96)80012-7
- Gillespie JP, Kanost MR, Trenczek T. 1997. Biological mediators of insect immunity. Annu Rev Entomol. 42:611-643. https://doi.org/10.1146/annurev.ento.42.1.611
- Hannig G, Makrides SC. 1998. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16:54-60.
- Hikima S, Hikima JI, Rojtinnakorn J, Hirono I, Aoki T. 2003. Characterization and function 301 of kuruma shimp lysozyme possessing lytic activity againts Vibrio species. Gene. 302 316:187-195.
- Hoffmann JA, Hetru C, Reichhart JM. 1993. The humoral antibacterial response of Drosophila. FEBS Lett. 325:63-66. https://doi.org/10.1016/0014-5793(93)81414-U
- Hultmark D. 1996. Insect lysozymes. EXS. 75:87-102.
- Hultmark D, Engstrom A, Anderson K, Steiner H, Bennich H, Boman HG. 1983. Insect immunity: attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 2:571-576.
- Jain D, Nair DT, Swaminathan GJ, Abraham EG, Nagaraju J, and Salunke DM. 2001 310 Structure of the induced antibacterial protein from Tasar silkworm, Anthemea mylitta: 311 Implications to molecular evolution. J Biol Chem. 276:41377-41382. https://doi.org/10.1074/jbc.M104674200
- Jenny RJ, Mann KG, Lundblad RL. 2003. A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa. Protein Expr Purif. 31:1-11. https://doi.org/10.1016/S1046-5928(03)00168-2
- Jolles P, Jolles J. 1984. What's new in lysozyme research? Mol Cell Biochem. 63:165-189.
- Kane JF. 1995. Effects of rare codon clusters on high-level expression of heterologous 316 proteins in Escherichia coli. Curr Opin Biotech. 6:494-500. https://doi.org/10.1016/0958-1669(95)80082-4
- Kim JW, Yoe SM. 2008. Cloning and prokaryotic expression of c-type lysozyme gene from Agrius convolvui. Animal Cells and Systems. 12:149-155. https://doi.org/10.1080/19768354.2008.9647168
- Kim JW, Yoe SM 2009. Isolation and characterization of the c-type lysozyme gene from the common cutworm, Spodoptera litura. Animal Cells and Systems. 13:345-350. https://doi.org/10.1080/19768354.2009.9647228
- LaVallie ER, McCoy JM. 1995. Gene fusion expression systems in Escherichia coli. Curr Opin Biotechnol. 6:501-506. https://doi.org/10.1016/0958-1669(95)80083-2
- Lemaitre B, Hoffmann J. 2007. The host defense of Drosophila melanogaster. Annu Rev Immunol. 25:697-743. https://doi.org/10.1146/annurev.immunol.25.022106.141615
- Liu Y, Zhao TJ, Yan YB, Zhou HM. 2005. Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr Purif. 44:155-161. https://doi.org/10.1016/j.pep.2005.03.030
- Makrides SC. 1996. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev. 60:512-538.
- Matsuura A, Yao M, Aizawa T, Koganesawa N, Masaki K, Miyazawa M, Demura M, Tanaka I, Kawano K, Nitta K. 2002. Structural analysis of an insect lysozyme exhibiting catalytic efficiency at low temperatures. Biochemistry. 41:12086-12092. https://doi.org/10.1021/bi016099j
- McNulty DE, Claffee BA, Huddleston MJ, Kane JE 2003. Mistranslational errors associated with the rare arginine codon CGG in Escherichia coli. Protein Expr Purif. 27:365-374. https://doi.org/10.1016/S1046-5928(02)00610-1
- Nomine Y, Ristriani T, Laurent C, Lefevre J, Weiss E, Trave G. 2001. A strategy for optimizing the mondispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein. Protein Eng. 14:297-305. https://doi.org/10.1093/protein/14.4.297
- Powning RF, Davidson WJ. 1973. Studies on insect bacteriolytic enzymes-I. Lysozyme in haemolymph of Galleria mellonella and Bombyx mori. Comp Biochem Phys B. 45:669-681. https://doi.org/10.1016/0305-0491(73)90205-8
- Regel R, Matioli SR, Terra WR. 1998. Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function. Insect Biochem Molec. 28:309-319. https://doi.org/10.1016/S0965-1748(97)00108-2
- Rossignol PA, Lueders AM. 1986. Bacteriolytic factor in the salivary glands of Aedes aegypti. Comp Biochem Phys B. 83:819-822. https://doi.org/10.1016/0305-0491(86)90153-7
- Rudolph R, Lilie H. 1996. In vitro folding of inclusion body proteins. FASEB J 10:49-56. https://doi.org/10.1096/fasebj.10.1.8566547
- Saluta M, Bell PA. 1998. Troubleshooting GST fusion protein expression in E. coli. Life Sci News. 1:1-3.
- Smith DB, Johnson KS. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathion S-transferase. Gene. 67:31-40. https://doi.org/10.1016/0378-1119(88)90005-4
- Sonomi H, Junichi H, Jiraporn R, Ikuo H, Takashi A. 2003. Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. Gene. 316:187-195. https://doi.org/10.1016/S0378-1119(03)00761-3
- Sorensen HP, Mortensen KK. 2005. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact. 4:1. https://doi.org/10.1186/1475-2859-4-1
- Spies AG, Karlinsey JE, Spence KD. 1986. Antibacterial hemolymph proteins of Manduca sexta. Comp Biochem Phys. 83:125-133. https://doi.org/10.1016/0300-9629(86)90099-X
- Stoscheck CM. 1990. Quantitation of protein. Methods Enzymol. 182:50-69.
- Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA. 76:4350-4354. https://doi.org/10.1073/pnas.76.9.4350
- van den Berg B, Ellis RJ, Dobson CM. 1999. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18:6927-6933. https://doi.org/10.1093/emboj/18.24.6927
- Waugh DS. 2005. Making the most of affinity tags. Trends Biotechnol. 23:316-320. https://doi.org/10.1016/j.tibtech.2005.03.012
- Yasin B, Pang M, Turner JS, Cho Y, Dinh NN, Waring AJ, Lehrer RI, Wagar E. 2000. Evaluation of the inactivation of infectious herpes simplex virus by host defense peptides. Eur J Clin Microbiol. 19:187-194. https://doi.org/10.1007/s100960050457
- Zasloff M. 2002. Antimicrobial peptides of multicellular organisms. Nature. 415:389-395. https://doi.org/10.1038/415389a
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