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Gonyaulax

The intensity of bioluminescence emission is > 2 x 10 photon /s-cm in the dinoflageUate Gonyaulax and the spectmm of light emission ranges from 450—490 nm (blue) in deep sea species, 490—520 nm (green) in coastal water species, and 510—580 nm (yeUow-green) in terrestrial and freshwater species. [Pg.271]

Gonyaulax. Gonjaulaxpolyedra flashes of light (0.1 s) from aumerous small (0.5 )dm) sciatUloas (234). These coataia an open... [Pg.273]

Since the year 2001, the species name Lingulodinium polyedrum (Stein) Dodge 1989 is widely used in place of Gonyaulax polyedra Stein 1883. Considering that many important papers on dinoflagel-late luminescence have been published using the old name, the name Gonyaulax is used in this book. [Pg.249]

Fig. 8.1 Luminescence spectra of luciferin-luciferase reaction of the dinoflagellate Gonyaulax polyedra (Lingulodinium polyedrum) in a solution (solid line), isolated scintillons (x), and living Gonyaulax cells (o). From Hastings et al., 1966. Fig. 8.1 Luminescence spectra of luciferin-luciferase reaction of the dinoflagellate Gonyaulax polyedra (Lingulodinium polyedrum) in a solution (solid line), isolated scintillons (x), and living Gonyaulax cells (o). From Hastings et al., 1966.
Fig. 8.2 Gel filtration on a column of Sephadex G-100 at pH 8 (both panels) of the crude extract of Gonyaulax polyedra cells prepared at pH 8 (upper panel) and prepared at pH 6 (lower panel). The activities of the 35 kDa and 130 kDa luciferases are measured by the addition of an excess of luciferin at pH 6.3 ( ) or at pH 8(A). The activity of the luciferin-bound LBP (luciferin-binding protein) in the upper panel is measured after the addition of an excess of 35 kDa luciferase at pH 6.3 ( ). In the lower panel, the LBP activity can be obtained by the addition of an excess of luciferin at pH 8, followed by the removal of unbound luciferin with a small column of Sephadex G-25 before the luminescence assay of bound luciferin at pH 6.3 (see the Section 8.2.8). The Overlap in the upper panel is the light emission resulting from the mixing of an aliquot of the fractions with pH 6.3 buffer. From Fogel and Hastings, 1971, with permission from Elsevier. Fig. 8.2 Gel filtration on a column of Sephadex G-100 at pH 8 (both panels) of the crude extract of Gonyaulax polyedra cells prepared at pH 8 (upper panel) and prepared at pH 6 (lower panel). The activities of the 35 kDa and 130 kDa luciferases are measured by the addition of an excess of luciferin at pH 6.3 ( ) or at pH 8(A). The activity of the luciferin-bound LBP (luciferin-binding protein) in the upper panel is measured after the addition of an excess of 35 kDa luciferase at pH 6.3 ( ). In the lower panel, the LBP activity can be obtained by the addition of an excess of luciferin at pH 8, followed by the removal of unbound luciferin with a small column of Sephadex G-25 before the luminescence assay of bound luciferin at pH 6.3 (see the Section 8.2.8). The Overlap in the upper panel is the light emission resulting from the mixing of an aliquot of the fractions with pH 6.3 buffer. From Fogel and Hastings, 1971, with permission from Elsevier.
Fig. 8.3 Effect of pH on the bioluminescence of Gonyaulax luciferin in the presence of 130 kDa luciferase (top) and 35 kDa luciferase (bottom) light intensity at 1 min ( ), and total light (o). From Hastings and Dunlap, 1986, with permission from Elsevier. Fig. 8.3 Effect of pH on the bioluminescence of Gonyaulax luciferin in the presence of 130 kDa luciferase (top) and 35 kDa luciferase (bottom) light intensity at 1 min ( ), and total light (o). From Hastings and Dunlap, 1986, with permission from Elsevier.
Luciferin binding protein (LBP) binds luciferin at pH 8 but not at pH 6 (Fogel and Hastings, 1971) thus, LBP inhibits the luciferin-luciferase reaction at pH 8 but not at pH 6. Luciferin bound to LBP is stable, differing from the free form of luciferin that is extremely unstable. The molecular size of the Gonyaulax LBP was considered... [Pg.264]

Bae, Y. M., and Hastings, J. W. (1994). Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga. Gonyaulax polyedra. Biochim. Biophys. Acta 1219 449-456. [Pg.381]

Bode, V. C., and Hastings, J. W. (1963). The purification and properties of the bioluminescent system in Gonyaulax polyedra. Arch. Biochem. Biophys. 103 488-499. [Pg.383]

DeSa, R., and Hastings, J. W. (1968). The characterization of scintillons. Bioluminescent particles from the marine dinoflagellate, Gonyaulax polye-dra.J. Gen. Physiol. 51 105-122. [Pg.391]

Dunlap, J. C. (1979). Circadian organization of bioluminescence in Gonyaulax polyedra. Ph.D. Dissertation, Harvard University, Cambridge, MA. [Pg.392]

Hastings, J. W., and Sweeney, B. M. (1957). The luminescence reaction in extracts of the marine dinoflagellate, Gonyaulax polyedra. J. Cell. Comp. Physiol. 49 209-226. [Pg.401]

Lee, D. H., et al. (1993). Molecular cloning and genomic organization of a gene for luciferin-binding protein from the dinoflagellate Gonyaulax polyedra. J. Biol. Chem. 268 8842-8850. [Pg.413]

Li, L. (2000). Gonyaulax luciferase gene structure, protein expression, and purification from recombinant sources. Method. Enzymol. 305 249-258. [Pg.415]

Li, L., and Hastings, J. W. (1998). The structure and organization of the luciferase gene in the photosynthetic dinoflagellate Gonyaulax polyedra. Plant Mol. Biol. 36 275-284. [Pg.415]

Morse, D., Pappenheimer, A. M., Jr., and Hastings, J. W. (1989). Role of luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra.]. Biol. Chem. 264 11822-11826. [Pg.421]

Seliger, H. H., Biggley, W. H., and Swift, E. (1969). Absolute values of photon emission from the marine dinoflagellates Pyrodinium bahamense, Gonyaulax polyedra and Pyrocystis lunula. Photochem. Photobiol. 10 227-232. [Pg.432]

Saxitoxin was first isolated from Alaskan butter clam Saxidomus giganteuSy but is actually produced by the dinoflagellate, Gonyaulax spp (i,2). More than a dozen related toxins have been isolated by several groups including ours (i). All of the toxins have the same unique tricyclic perhydropurine skeleton, and there were various speculations about the origin of the perhydropurine ring (I). [Pg.21]

Rapid-acting paralytic neurotoxins that blocks transient sodium channels and inhibits depolarization of nerve cells. They are some of the causative agents of paralytic shellfish poisoning (PSP). They are obtained from dinoflagellates (Gonyaulax spp., Alexandrium spp.) and cyanobacteria (Anabaena circinalis). [Pg.473]

Circadian rhythm of total protein synthesis— cytoplasm and chloroplasts of Gonyaulax polyhedra Sulfate incorporation in Udotea petiolata thalli Photosynthetic activity of phytoplankton Thymidine incorporation into Nostoc Chloroplast nucleoids of Zea mays Localization of chloroplast binding protein in cells of wheat leaves Distributon of [14C]-dichlorophenoxyacetic acid Donner et al. (13) Mariani and Favoli (14) Bourdier and Bohatier (15) Favoli and Grilli (16) Lindbeck et al. (17) Bronsema et al. (18)... [Pg.254]

Surprisingly, most of the definitive cell biology on toxic dino-flagellates has yet to be observed, understood and described. What was once thought to be the major causative genus, Gonyaulax, is now known to contain a wide variety of similar strains/ varieties/species ( ). ... [Pg.9]

Station 5 is nearshore. Station 1 is approximately 25 miles offshore. Summer (July) 1979. After Holligan et al. (submitted) (8). Gonyaulax tamarensis var. excavata comprised a major percent of phytoplankton biomass from 0-60 m. Station 5 = 0% station 4 = 307o station 3 = 467 station 2 = 47 station 1 = 07o. [Pg.12]

Figure 5. Pigment per cell of Gonyaulax tamerensis var excavata grown under 1007o (266 juEin cm s ) and 25% (66 juEin cm - )... Figure 5. Pigment per cell of Gonyaulax tamerensis var excavata grown under 1007o (266 juEin cm s ) and 25% (66 juEin cm - )...
Figure 6. Diagram of chloroplast size and shape observed using epifluorescence microscopy. Gonyaulax tamarensis var. excavata-A. grown at 266 pEin cm s l and B. at 50%, or 133 juEin cm s . ... Figure 6. Diagram of chloroplast size and shape observed using epifluorescence microscopy. Gonyaulax tamarensis var. excavata-A. grown at 266 pEin cm s l and B. at 50%, or 133 juEin cm s . ...

See other pages where Gonyaulax is mentioned: [Pg.641]    [Pg.249]    [Pg.249]    [Pg.252]    [Pg.344]    [Pg.387]    [Pg.395]    [Pg.415]    [Pg.461]    [Pg.29]    [Pg.36]    [Pg.79]    [Pg.291]    [Pg.474]    [Pg.475]    [Pg.662]    [Pg.162]   
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See also in sourсe #XX -- [ Pg.410 ]

See also in sourсe #XX -- [ Pg.84 , Pg.85 ]




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Gonyaulax catenella

Gonyaulax catenella mussels

Gonyaulax dinoflagellate

Gonyaulax excavata

Gonyaulax polyedra

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Gonyaulax spp

Gonyaulax tamarensis

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The Luciferase of Gonyaulax polyedra

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