. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 346 O. SHIMOMURA ET AL. 300 5 200 - JS 100 -. O Luciferase A D Luciferase B A Luciferase C O Luciferase L 0123 Concentration of coelenterazine () Figure 8. Effect of coelenterazine concentration on the luminescence catalyzed by luciferases A. B, C, and L. The measurements were done in the standard buffer. The amounts of sample used were the same as in Figure 6 for luciferases A, B, and C. The data for luciferase L were taken from the previous report (Shimomura and Flood. 1998). as those found in the adult medusae (Flood,
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 346 O. SHIMOMURA ET AL. 300 5 200 - JS 100 -. O Luciferase A D Luciferase B A Luciferase C O Luciferase L 0123 Concentration of coelenterazine () Figure 8. Effect of coelenterazine concentration on the luminescence catalyzed by luciferases A. B, C, and L. The measurements were done in the standard buffer. The amounts of sample used were the same as in Figure 6 for luciferases A, B, and C. The data for luciferase L were taken from the previous report (Shimomura and Flood. 1998). as those found in the adult medusae (Flood, unpubl. obs.). The decrease of luciferase in the eggs, described above, is puzzling and intriguing. Why does the egg contain a large amount of luciferase in the first place? What is the function or purpose of this luciferase? A similar phenomenon has been observed in the eggs of bioluminescent hydrozoan medusas that contain a Ca~ sensive photoprotein, a complex of oxygenated coelentera- zine and an enzyme. In those eggs, the amount of photo- protein slowly declines during the development of the planula larva, and then markedly declines when the planula undergoes metamorphosis to become a polyp (Freeman and Ridgway, 1987). Properties of luciferases A, B, and C The present results indicate that luciferases B (40 kDa) and C (80 kDa) are the dimer and tetramer. respectively, of the luciferase A monomer (20 kDa). The specific lumines- cence activities of luciferases A, B, and C were in a range of — X 1016 photons/s, showing a tendency to in- crease slightly as the oligomer size increases. This is the highest specific activity ever reported for a luciferase whose substrate is coelenterazine; the highest in the past was that of the luciferase of the deep-sea shrimp Oploplwms ( X 101"1 photons/s) (Shimomura et ai, 1978). The specific activity of purified luciferases A. B, and C can vary in a complex manner, depending upon the method of purification and the history of h
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