Luciferase properties

Although most anesthetics are achiral or are adininistered as racemic mixture, the anesthetic actions are stereoselective. This property can define a specific, rather than a nonspecific, site of action. Stereoselectivity is observed for such barbiturates as thiopental, pentobarbital, and secobarbital. The (3)-enantiomer is modestly more potent (56,57). Additionally, the volatile anesthetic isoflurane also shows stereoselectivity. The (3)-enantiomer is the more active (58). Further evidence that proteins might serve as appropriate targets for general anesthetics come from observations that anesthetics inhibit the activity of the enzyme luciferase. The potencies parallel the anesthetic activities closely (59,60). 

Properties of the luciferases. According to Shimomura and Flood (1998) and Shimomura et al. (2001), all Periphylla luciferases L, A, B and C catalyze the oxidation of coelenterazine, resulting in the emission of blue light (Amax 465 nm). Luciferases B (40 kDa) and C (80 kDa) are apparently the dimer and tetramer, respectively, of luciferase A (20 kDa). The presence of a salt is essential for the activity of luciferase, and the optimum salt concentration is about 1M in the case of NaCl for all forms of luciferases. The luminescence intensity of luciferase L is maximum near 0°C, and decreases almost linearly with rising temperature, falling to zero intensity at 60°C the luminescence intensity profiles of luciferases A, B and C show their peaks at about 30°C (Fig. 4.5.3). The Michaelis constants estimated for luciferases A, B and C with coelenterazine are all about 0.2 xM, and that for luciferase L is 1.2 jiM. 

Properties of Latia luciferase and the purple protein. The absorption spectra of purified Latia luciferase and the purple protein are shown in Fig. 6.1.4. The sedimentation coefficient (sjo) of the... 

Ballou, B., Szent-Gyorgyi, C., and Finley, G. (2000). Properties of a new luciferase from the copepod Gaussia princeps. 11th Int. Symp. on Biolumin. Chemilumin., Abstract p. 34. Asilomar, CA. 

Bellisario, R., Spencer, T. E., and Cormier, M. J. (1972). Isolation and properties of luciferase, a non-heme peroxide from the bioluminescent earthworm, Diplocardia longa. Biochemistry 11 2256-2266. 

Choi, H., Tang, C.-K., and Tu, S. C. (1995). Catalytically active forms of the individual sub-units of Vibrio harveyi luciferase and their kinetic and binding properties./. Biol. Ghent. 270 16813-16819. 

DeLuca, M., and McElroy, W. D. (1978). Purification and properties of firefly luciferase. Method. Enzymol. 57 3-15. 

Gunsalus-Miguel, A., et al. (1972). Purification and properties of bacterial luciferases. J. Biol. Chem. 247 398-404. 

Hastings, J. W., Balny, C., Le Peuch, C., and Douzou, P. (1973). Spectral properties of an oxygenated luciferase-flavin intermediate isolated by low-temperature chromatography. Proc. Natl. Acad. Sci. USA 70 3468-3472. 

Kobayashi, K., et al. (2000). Purification and properties of the luciferase from the marine ostracod Vargula hilgendorfii. In Case, J. F., et al. (eds.), Biolumin. Chemilumin.,Proc. Int. Symp., 11th, pp. 87-90. World Scientific, Singapore. 

Matthews, J. C., Hori, K., and Cornier, M. J. (1977b). Substrate and substrate analogue binding properties of Renilla luciferase. Biochemistry 16 5217-5220. 

Nakamura, T., and Matsuda, K. (1971). Studies on luciferase from Photobacterium phosphoreum. 1. Purification and physical properties. /. Biochem. 70 35-44. 

Petushkov, V. N., Gibson, G. B., and Lee, J. (1995). Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates. Biochemistry 34 3300-3309. 

Shimomura, O., and Johnson, F. H. (1968c). Purification and properties of the luciferase and of a protein cofactor in the bioluminescence system of Latia neritoides. Biochemistry 7 2574-2580. 

Shimomura, O., etal. (2001). Isolation and properties of the luciferase stored in the ovary of the scyphozoan medusa Periphylla periphylla. Biol. Bull. 201 339-347. 

Tsuji, F. I., Lynch, R. V., Ill, and Stevens, C. L. (1974). Some properties of luciferase from the bioluminescent crustacean, Cypridina hilgendorfii. Biochemistry 13 5204-5209. 

Tu, S.-C. (1979). Isolation and properties of bacterial luciferase-oxygenated flavin intermediate complexed with long-chain alcohols. Biochemistry 18 5940-5945. 

Tu, S.-C. (1986). Bacterial luciferase 4a-hydroperoxyflavin intermediates stabilization, isolation, and properties. Method. Enzymol. 133 128-139. 

Bacterial bioluminescence, 30-46 factors required, 31 general scheme, 32 in vivo luminescence, 41 luminescence reaction, 37, 38 Bacterial luciferase, 33-35, 343 assay, 39 cloning, 34 crystal structure, 34 extraction and purification, 34 inactivation, 34, 35 molecular weight, 34 properties, 34 storage, 35 subunits, 34... 

Balanoglossus luciferase, 315 extraction, 315 Balanoglossus luciferin, 316 extraction, 316 Basidiomycetes, 266 Bathophilus, 338 Beneckea, 31, 33, 34, 333 Bentbalbella, 339 Benthosema, 339 2-Benzylimidazopyrazinone, 168 Beroe, 155, 334 Berovin, 155, 346 extraction and purification, 155 spectral properties, 156 BFP, 101... 

Cypridina luciferase, 62-64, 343 cloning, 63 inhibitors, 63 molecular weight, 63 properties, 63, 64 purification, 62 turnover rate, 68... 

The present book describes all the significant studies and findings on the chemistry of the more than 30 different bioluminescent systems presently known, accompanied by over 1000 selected references. It includes descriptions of the purification and properties of bioluminescent compounds, such as luciferins, luciferases and photoproteins, and the mechanisms of luminescence reactions. To make the book more useful than a mere review volume and to save researchers time in looking into original references, I have included a considerable amount of original experimental methods, data and graphs. In addition, I have included some new data and experimental methods unavailable elsewhere. I hope this volume will be useful to researchers and students, and it will be my greatest pleasure if this book contributes... 

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