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Jellyfish luminescent

The activity of an enzyme is responsible for the glow of the luminescent jellyfish at left. The enzyme aequorin catalyzes the oxidation of a compound by oxygen in the presence of calcium to release CO2 and light. [(Left) Fred Bavendam/Peter Arnold.]... [Pg.302]

Inouye and Shimomura, 1997). With Ptilosarcus luciferase, the luminescence intensity of e-coelenterazine is also significantly higher than that of coelenterazine. With other coelenterazine luciferases, however, the luminescence intensity of e-coelenterazine is generally lower than that of coelenterazine for example, the luminescence intensities of e-coeienterazine measured with the luciferases of the decapod shrimps, the jellyfish Periphylla, and the copepod Pleuromamma, were 50%, 4%, and 0.8%, respectively, in comparison with that of coelenterazine. Thus, the luminescence of coelenterazine catalyzed by Pleuromamma luciferase is suppressed by the addition of e-coelenterazine. [Pg.179]

British scientists immobilized53 in a porous sol-gel glass aequorin - the bioluminescent protein found in the jellyfish Aequorea aequorea. The luminescence from this protein is specifically triggered by the presence of calcium ions. The intensity of the luminescence, measured at the peak... [Pg.365]

Our retina has red, green, and blue cones which include rhodopsins as photoreceptors [6-8], Phytochromes are photo-sensors of green plants [9], Biological luminescences from fireflies [10] and some jellyfishes [11] are also beautiful activities of living organism. Recently, fluorescent proteins are routinely applied as molecular markers for gene expression in the field of molecular biology [12]. [Pg.94]

I filtered the mixture. The filtrate, now free of cells and debris, was nearly dark, but it regained its luminescence upon neutralization with a small amount of sodium bicarbonate. Indeed, the experiment showed that the luminescence substance of the jellyfish was extracted into the solution at pH 4. But my real surprise came next. When I added a small amount of sea water to the solution, its luminescence became explosively strong. Because the composition of seawater is known, I quickly discovered that the activator is Ca. The discovery of Ca. as the activator in turn suggested that EDTA should serve as a better inhibitor of luminescence than acidification. Based on this information, we devised a method of extracting the light-emitting principle. We collected and extracted about 10,000 jellyfish in that summer. [Pg.29]

Name for natural compounds that exhibit biolumines-cence under the action of appropriate enzymes ( luci-ferases). The L. occurring in different organisms (bacteria, crabs, mussels, jellyfish, deep-sea fish, worms, beetles, etc.) have completely different structures. Cy--pridina species (ostracods), e. g., Cypridina hilgendor-fii, living on the Pacific coasts contain a pyrazine derivative (Cypridina L) C22H27N7O, Mr 405.50 as L. Cypridina L. exists, depending on the pH value, in three tautomeric forms. The kinetics of Cypridina luminescence are of first order, this represents the simplest bi-oluminescence system ... [Pg.367]

If luminescence is a result of a biochemical reaction, the principle is called bioluminescence. The most frequently used bioluminescence system is that of the firefly. The enzyme luciferase catalyses the oxidation of luciferin as a substrate in the presence of adenosine triphosphate (ATP) (Scheme 7). Another bioluminescence system makes use of a luciferase from certain marine bacteria. A long-chain aldehyde is oxidized in the presence of luciferase, an oxido-reductase and NAD/NADH. Recently, a photoprotein isolated from the bioluminescent jellyfish Aequorea victoria, has been found to be an efficient bioluminescence label for immunoassays. [Pg.2182]


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