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Academic literature on the topic 'Renilla reniformis'
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Journal articles on the topic "Renilla reniformis"
Liu, Jingxue, Dennis J. O'Kane, and Alan Escher. "Secretion of functional Renilla reniformis luciferase by mammalian cells." Gene 203, no. 2 (December 1997): 141–48. http://dx.doi.org/10.1016/s0378-1119(97)00505-2.
Full textTursch, Bernanrd, Helio Barreto, and Nikolai Sharapin. "Occurence of Cholesterol in Renilla Reniformis and Echinometra Lucunter." Bulletin des Sociétés Chimiques Belges 72, no. 11-12 (September 2, 2010): 807–8. http://dx.doi.org/10.1002/bscb.19630721116.
Full textKeifer, Paul A., Kenneth L. Rinehart, and Irving R. Hooper. "Renillafoulins, antifouling diterpenes from the sea pansy Renilla reniformis (Octocorallia)." Journal of Organic Chemistry 51, no. 23 (November 1986): 4450–54. http://dx.doi.org/10.1021/jo00373a020.
Full textLorenz, W. W., R. O. McCann, M. Longiaru, and M. J. Cormier. "Isolation and expression of a cDNA encoding Renilla reniformis luciferase." Proceedings of the National Academy of Sciences 88, no. 10 (May 15, 1991): 4438–42. http://dx.doi.org/10.1073/pnas.88.10.4438.
Full textLoening, Andreas Markus, Anna M. Wu, and Sanjiv Sam Gambhir. "Red-shifted Renilla reniformis luciferase variants for imaging in living subjects." Nature Methods 4, no. 8 (July 8, 2007): 641–43. http://dx.doi.org/10.1038/nmeth1070.
Full textLoening, Andreas Markus, Timothy David Fenn, and Sanjiv Sam Gambhir. "Crystal Structures of the Luciferase and Green Fluorescent Protein from Renilla reniformis." Journal of Molecular Biology 374, no. 4 (December 2007): 1017–28. http://dx.doi.org/10.1016/j.jmb.2007.09.078.
Full textInouye, Satoshi. "Expression, purification and characterization of calcium-triggered luciferin-binding protein of Renilla reniformis." Protein Expression and Purification 52, no. 1 (March 2007): 66–73. http://dx.doi.org/10.1016/j.pep.2006.07.028.
Full textKumar, Santosh, Maria Harrylock, Kenneth A. Walsh, Milton J. Cormier, and Harry Charbonneau. "Amino acid sequence of the Ca2+ -triggered luciferin binding protein of Renilla reniformis." FEBS Letters 268, no. 1 (July 30, 1990): 287–90. http://dx.doi.org/10.1016/0014-5793(90)81029-n.
Full textLuker, Gary D., J. Patrick Bardill, Julie L. Prior, Christina M. Pica, David Piwnica-Worms, and David A. Leib. "Noninvasive Bioluminescence Imaging of Herpes Simplex Virus Type 1 Infection and Therapy in Living Mice." Journal of Virology 76, no. 23 (December 1, 2002): 12149–61. http://dx.doi.org/10.1128/jvi.76.23.12149-12161.2002.
Full textSrikantha, T., A. Klapach, W. W. Lorenz, L. K. Tsai, L. A. Laughlin, J. A. Gorman, and D. R. Soll. "The sea pansy Renilla reniformis luciferase serves as a sensitive bioluminescent reporter for differential gene expression in Candida albicans." Journal of bacteriology 178, no. 1 (1996): 121–29. http://dx.doi.org/10.1128/jb.178.1.121-129.1996.
Full textDissertations / Theses on the topic "Renilla reniformis"
盧三吉. "Fed-Batch Fermentation for Recombinant E.coli Cultivation to Produce Renilla Reniformis Luciferase." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/06715802774221419015.
Full text國立臺灣科技大學
化學工程系
92
Abstract Renilla riniformis luciferase can catalyze Coelenterazine to light and has many application in the field of industry. In this thesis,we use recombinant E.coli BL21(DE3)/pETRlu and several expressing strains constructed based on BL21(DE3)/ pETRlu to express Renilla riniformis luciferase.The effects of carbon source、nitrogen source and several lactose induction strategies on the expression efficiency,and production concentration of luciferase were studied.With lactose (5/1/1) induction at late log-phase (OD600=5.433) of BL21(DE3)/pETRlu, luciferase of 1.16g/L could be obtained at the end of 14h batch fermentation.Besides,fed-batch fermentation with exponential feeding strategy had been carried out,high cell density (OD600=35) was obtained but the luciferase production (0.7g/L) was not enhanced.In the fed-batch fermentation with pH-stat feeding strategy,cell density of OD600=85.6 was obtained and luciferase concentration of 11.89g/L could be obtained at the end of 21h.
tsang-te, chiu, and 邱倉德. "Fusion Renilla reniformis luciferase with VHb to enhance its activity and productivity." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/30365617232251169872.
Full text國立臺灣科技大學
化學工程系
93
Renilla riniformis luciferase (RLuc) catalyzes coelenterazine oxidation to produce light. RLuc gene was expressed in E. coli to facilitate the large-scale production of RLuc. RLuc gene of 1 to 3 copies were cloned to the very stable F-plasmid and named as pBAC-1xRLuc, pBAC-2xRLuc, and pBAC-3xRLuc. The expression of RLuc was driven by the strong T7 promoter. The expression level of pBAC-3xRLuc was higher than two others, but lower than the pET expression vector. RLuc activity was strongly inhibited by imidazole employed in IMAC. Removing imidazole resumed RLuc activity to about 83.21 percentage. O2 plays a very important role in the RLuc catalyzed oxidation. Vitreoscilla hemoglobin (VHb) is able to bind O2. RLuc fused with VHb enhanced its activity by 2 fold. Besides, the fused VHb still retained its activity which also enhanced the cells growth. As a consequence, the productivity of RLuc activity was enhanced bye fusing with VHb.