View options
Result details

Results per page
Articles per page View Sort by

1 results matched your search query
Keywords = Vitreoscilla hemoglobin

  • Open Access Research Article
    Export citation: APA   BibTeX   EndNote   RIS  
    Trends Journal of Sciences Research 2015, 2(4), 134-140. http://doi.org/10.31586/Biology.0204.04
    13 Views 37 Downloads PDF Full-text (733.934 KB)  HTML Full-text
    Abstract
    Methionine, a sulfur amino acid, is the first amino acid that is required for many proteins, during synthesis. Our preliminary studies showed that this compound was produced during the late (post-stationary) secondary phase of growth. Therefore, restriction of methionine may be a useful strategy in limiting cancer growth. The bacterial
    [...] Read more.
    Methionine, a sulfur amino acid, is the first amino acid that is required for many proteins, during synthesis. Our preliminary studies showed that this compound was produced during the late (post-stationary) secondary phase of growth. Therefore, restriction of methionine may be a useful strategy in limiting cancer growth. The bacterial strain used in this study was Citrobacter freundii (NRRL B-2643) and their vgb+ recombinant strain. A 1/100 inoculum of overnight cultures grown in LB was made in 50 ml LB in 150 ml Erlenmeyer flasks. Inocula in flasks were grown for 24 h at 30 ?C in a 200 rpm water-bath. For MGL production, 250 ?L of this O/N culture was then inoculated into 150 mL conical flask containing 50 mL of sterile mineral salts medium supplemented with 1 % or 0.1 % (w/v) glucose, respectively. This was incubated for 96 h at 30 ?C, 200 rpm on an orbital shaker. The highest MGL concentration (2,02) was reached by the recombinant strain of Cf[pUC8:15] 72 h after the start of incubation MM+0,1% glucose source. In comparison, the wild type strain produced 3,14 of MGL concentration 72 h was reached MM+0,1% glucose source. The poor media and secondary phase (72 h and up) was used to for MGL production. This is more appropriate. Plasmid is disadvantages in the secondary stage.  Full article
    Figures

    Figure 1 of 5

    References
    [1]
    Cavuoto P, Fenech M.F. (2012). A review of methionine dependency and the role of methionine restriction in cancer growth control and life-span extension. Cancer Treatment Rev. 38, 726-736.
    [2]
    Sato D, Nozaki T. (2009). Methionine Gamma-Lyase: The unique reaction mechanism, physiological roles, and therapeutic applications against infectious diseases and cancers. IUBMB Life. 61(11), 1019-1028.
    [3]
    Kudou D, Misaki S, Yamashita M, Tamura T, Esaki N, Inagaki K. (2008). The role of cysteine 116 in the active site of the antitumor enzyme L-methionine ?-lyase from Pseudomonas putida. Biosci Biotechnol Biochem. 72(7), 1722- 1730.
    [4]
    Morozova E.A., Kulikova V.V., Yashin D.V., Anufrieva N.V., Anisimova N.Y., Revtovich S.V., Kotlov M.I., Belyi Y.F., Pokrovsky V.S., Demidkina T.V. (2013). Kinetic Parameters and cytotoxic activity of recombinant methionine ?-lyase from Clostridium tetani, Clostridium sporogenes, Porphyromonas gingivalis and Citrobacter freundii. Acta Naturae. 5(3), 92-98.
    [5]
    Lua S, Chena G.L., Rena C, Kwabi-Addob B, Epner D.E. (2003). Methionine restriction selectively targets thymidylate synthase in prostate cancer cells. Biochem Pharm. 66, 791-800.
    [6]
    Saa L, Mato J.M., Pavlov V. (2012). Assays for methionine ?- lyase and S-adenosyl-L-homocysteine hydrolase based on enzymatic formation of CdS quantum dots in situ. Anal Chem, 84, 8961-8965.
    [7]
    Revtovich S.V., Morozova E.A., Khurs E.N., Zakomirdina L.N., Nikulin A.D., Demidkina T.V., Khomutov R.M. (2011). Three dimensional structures of noncovalent complexes of Citrobacter freundii methionine ?-lyase with substrates. Biochemistry, 76(5), 564-570.
    [8]
    Benavide M.A., Oelschlager D.K., Zhang H.G., Stockard C.R., Vital-Reyes V.S., Katkoori V.R., Manne U, Wang W, Bland K.I., Grizzle W.E. (2007). Methionine inhibits cellular growth dependent on the p53 status of cells. Am J Surgery. 193, 274- 283.
    [9]
    Li H, Huang Y, Zhang J, Du J, Tan H, Lu Y., Zhou, S. (2011). Identification and characterization of a novel methionine ?-lyase gene from deep-sea sediment metagenomic library. World J Microbiol Biotechnol. 27, 2729-2736.
    [10]
    Morozova E.A., Bazhulina N.P., Anufrieva N.V., Mamaeva D.V., Tkachev Y.V., Streltsov S.A., Timofeev V.P., Faleev N.G., Demidkina T.V. (2010). Kinetic and spectral parameters of interaction of Citrobacter freundii methionine ?-lyase with amino acids. Biochemistry. 7(10), 1272-1280.
    [11]
    Ronda L, Bazhulina N.P., Morozova E.A., Revtovich S.V., Chekhov V.O., Nikulin A.D., Demidkina T.V., Mozzarelli A. (2011). Exploring methionine ?-lyase structure-function relationship via microspectrophotometry and X-ray crystallography. Biochim Biophys Acta. 1814, 834-842.
    [12]
    Surowsky B, Fr?hling A, Gottschalk N, Schl?ter O, Knorr D. (2014). Impact of cold plasma on Citrobacter freundii in apple juice: Inactivation kinetics and mechanisms. Int J Food Microbiol. 174, 63-71.
    [13]
    Wanga Z, Xiao Y, Chen W, Tang K, Zhang L. (2009). Functional expression of Vitreoscilla hemoglobin (VHb) in Arabidopsis relieves submergence, nitrosative, photo-oxidative stress and enhances antioxidants metabolism. Plant Science. 176, 66-77.
    [14]
    Soda K. (1968). Microdetermination of D-amino acids and D- amino acid oxidase activity with 3-methyl-2-benzothiazolone hydrazone hydrochloride. Anal Biochem. 25, 228-235.
    [15]
    Tanaka H, Imahara H, Esaki N, Soda K. (1980). Selective determination of L-methionine and L-cysteine with bacterial L-methionine ?-lyase and anti-tumor activity of the enzyme. J Appl Biochem. 2, 439-444.
    [16]
    Kahraman H, Erenler S.O. (2012). Rhamnolipid production by Pseudomonas aeruginosa engineered with the Vitreoscilla hemoglobin gene. Appl Biochem Microbiol. 48(2), 188-193.
    [17]
    Pavillard V, Nicolaou A, Double J.A., Phillips R.M. (2006). Methionine dependence of tumours: A biochemical strategy for optimizing paclitaxel chemosensitivity in vitro. Biochem Pharma. 71, 772-778.
Filter options
Publication Date
From to
Refine Publication Date
Subject Areas
Refine Subjects
Article Types
Refine Article Types
Countries / Territories
Refine Countries / Territories