Biopolym. Cell. 2002; 18(6):529-533.
http://dx.doi.org/10.7124/bc.000631
Molecular and Cell Biotechnologies
The influence of nutrients in growth media on the lysis and extracellular localization of human alpha interferon in the system of recombinant proteins overproduction using bacteriophage lambda
1Slavchenko I. Yu.
  1. PSRS "Biotechnolog"
    150, Akademika Zabolotnogo Str., Kyiv, Ukraine, 03680

Abstract

The influence of different carbon sources on the yield of extracellular human alpha interferon in the system of recombinant proteins biosynthesis using bacteriophage lambda was investigated. Both the level of target protein synthesis and productivity of infected cells lysis are shown to increase in the presence of certain carbon sources in the growth media. This results in rising the extracellular concentration of recombinant protein.
Full text: (PDF, in Russian)

References

[1] Ptashne M. A Genetic Switch: Gene Control and Phage A. Cell Press, Cambridge, MA, and Blackwell Scientific, Palo Alto, CA, 1986. 138 pp.
[2] Slavchenko IYu. The influence of temperature on the yield soluble human alpha interferon in the system of recombinant proteins overproduction using bacteriophage lambda. Biopolym Cell. 2002; 18(5):436-441.
[3] Moir A, Brammar WJ. The use of specialised transducing phages in the amplification of enzyme production. Mol Gen Genet. 1976;149(1):87-99.
[4] AS SSSR N 600175. Method of biosynthesis of biologically active substances. VA Kordium, SI Chernykh. Publ. in BI. N 12, 1978.
[5] Slavchenko IYu, Chernykh SI, Kordium VA. The study phagedependent synthesis b-lactamase in isogenic and Su Su + E. coli strains during infection of phages Xbla and XblaQ'R'. Enzymes of microorganisms. M.: VNII-SENTI, 1989; 31-6.
[6] Slavchenko IYu. Study bacteriophage ? efficiency for human a2 interferon production in Escherichia coli. Auth. Thesis. ... kand biol nauk. Kiev, 1990. 19 p.
[7] Pat Ukraine N 2463. A method of producing b-galactosidase. VA Kordium, SI Chernykh, IYu Slavchenko, VG Korobko. Publ. in BI N 5-1, 1994.
[8] Schwartz M. The adsorption of coliphage lambda to its host: effect of variations in the surface density of receptor and in phage-receptor affinity. J Mol Biol. 1976;103(3):521-36.
[9] Garrett JM, Young R. Lethal action of bacteriophage lambda S gene. J Virol. 1982;44(3):886-92.
[10] Roe JH, Record MT Jr. Regulation of the kinetics of the interaction of Escherichia coli RNA polymerase with the lambda PR promoter by salt concentration. Biochemistry. 1985;24(18):4721-6.
[11] Gabig M, Herman-Antosiewicz A, Kwiatkowska M, Los M, Thomas MS, Wegrzyn G. The cell surface protein Ag43 facilitates phage infection of Escherichia coli in the presence of bile salts and carbohydrates. Microbiology. 2002;148(Pt 5):1533-42.
[12] Gabig M, Obuchowski M, Wegrzyn A, Szalewska-Pa?asz A, Thomas MS, Wegrzyn G. Excess production of phage lambda delayed early proteins under conditions supporting high Escherichia coli growth rates. Microbiology. 1998;144 ( Pt 8):2217-24.
[13] Czyz A, Los M, Wrobel B, Wegrzyn G. Inhibition of spontaneous induction of lambdoid prophages in Escherichia coli cultures: simple procedures with possible biotechnological applications. BMC Biotechnol. 2001;1:1.
[14] Slavchenko IYu. Isolation of clones sensitive to bacteriophage ? from the phage resistant Escherichia coli strain. Biopolym Cell. 2001; 17(2):160-5.
[15] Slavchenko IYu. The expression of human alpha-2b interferon in different strains of Escherichia coli. Biopolym Cell. 2001; 17(6):546-50.
[16] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[17] Slavchenko IYu. The influence of organic carbon sources on the production of a recombinant protein in Escherichia coli cells. Biopolym Cell. 2002; 18(4):334-339.
[18] DNA cloning: a practical approach. Ed. DM Glover. Oxford, IRL Press, 1985; Vol. 1 and 2: 435 p