Bioluminescence: 2
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Glowing Plankton
GFP and luciferase in copepods
Marine organisms include various bioluminescent creatures. We have identified a green fluorescent protein (GFP) and a secreted luciferase (luminescent enzyme) from copepods, the most dominant plankton species.
Research
Zooplankton serves as energy transmitters in marine ecosystems, passing basic production to higher organisms. The dominant zooplankton species in the Arctic Ocean are copepods, most of which have a lifespan of one year or less, but their samples can be preserved semi-permanently with formalin fixation, making them an ideal taxonomic group for assessing the interannual variability in biological production in the region. Some species of copepods are also bioluminescent. It is thought that they emit light when they are about to be predated upon in dark waters, and use it to distract predators. We have identified a fluorescent protein (GFP) and a luciferase (luminescent enzyme) from copepods.
Atsushi Yamaguchi Associate Professor -
Liposomal Bioluminescence Immunoassay
Preparation of liposomes encapsulating luciferase and application as an ultra-sensitive label in immunoassays
We have encapsulated the enzyme luciferase (Luc), which catalyzes bioluminescence reactions, in liposome, a lipid bilayer vesicle, and applied it as an ultrasensitive label for immunoassays. As a model substance, we performed immunoassay of C-reactive protein, a marker of inflammation, and found that it could be quantified.
Research
Since immunoassay is an essential technology in clinical laboratories and for environmental analysis, technological advances (simplification, high sensitivity, high throughput, etc.) has come essential as the analytes are becoming more diverse and smaller. We aim to construct an ultra-sensitive immunoassay system in which the bioluminescent enzyme Luc is encapsulated in lipid bilayer membrane vesicles, called liposomes, and use it as a label in immunoassays. By encapsulating a large number of Luc in liposomes, it becomes possible to label antibodies in a stable state. However, although the method of encapsulating enzymes inside liposomes is already known, no studies have been done on Luc. In our study, we have encapsulated heat-stabilized recombinant Luc into liposomes and evaluated the amount and stability of the encapsulation. We have also constructed an immunoassay system for C-reactive protein using Luc-encapsulated liposomes as a label.
Hirofumi Tani Associate Professor
