Isolation and properties of Renilla reniformis luciferase, a low molecular weight energy conversion enzyme.
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Biomedical subjects
Publications and source records attributed to M J Cormier.
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The oxidation of luciferin catalyzed by sea pansy luciferase results in the emission of light. Molecular oxygen is required and carbon dioxide is produced. When the reaction occurs in the presence of H(2) (18)O, both of the oxygens of the carbon dioxide are labeled. One of the oxygens arises from the nonenzymic exchange of the ketone group of the substrate; the other oxygen is incorporated during the enzymic oxidation of the luciferin. When the reaction is carried out in the presence of (18)O(2), neither of the oxygens of the carbon dioxide is labeled. Thus the source of oxygen in the carbon dioxide is water. A mechanism for the oxidative reaction is proposed.
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2,6-Dibromophenol has been isolated from a luminous marine enteropneust, Balanoglossus biminiensis, found on intertidal beach areas at Sapelo Island, Georgia. This compound, responsible for the characteristic "iodoform-like" odor of these animals, is present in relatively large amounts; the estimated quantity per organism is 10 to 15 milligrams. Identity of the isolated substance as 2,6 dibromophenol is based on analyses of ultraviolet, infrared, and nuclear magnetic resonance spectra, mass spectrometry analysis, and on melting-point data.
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A cDNA encoding the Renilla reniformis luciferase was expressed in similan and murine cells in a transient and stable manner, respectively. Light emission catalyzed by luciferase was detected from transfected cells both in vitro and in vivo. This work establishes the Renilla luciferase gene as a new efficient marker of gene expression in mammalian cells.