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Topic: Luciferin

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	Luciferin - Wikipedia, the free encyclopedia
		Luciferin is a generic name for light-emitting pigments found in organisms capable of bioluminescence, like fireflies, deep-sea fish and microbes.
		Luciferin is oxidized in the presence of the enzyme luciferase to produce oxyluciferin and energy in the form of light.
		Dinoflagellate luciferin is a chlorophyll derivative and is found in dinoflagellates (a type of marine plankton), and a very similar type is found in some types of euphausiid shrimp.
	en.wikipedia.org /wiki/Luciferin (169 words)

	BIOSYNTH : Substrates Producing Bioluminescence
		Luciferin is the most popular and versatile bioluminescent substrate.
		In vitro, the luciferase enzyme is assayed by the addition of luciferin, ATP and magnesium ions.
		It produces carbon dioxide and oxyluciferin in an excited state which decays quickly by emitting a yellow-green light (max 560 nm) with an amazingly high quantum yield of 0.88: microplate readers, standard luminometers, scintillation counters or special video cameras are all used as light detectors.
	www.biosynth.com /index.asp?topic_id=118&g=19&m=181 (524 words)

	[No title] (Site not responding. Last check: 2007-11-06)
		Luciferases, are oxygenases, that act on a substrate, luciferin, in the presence of mole- cular oxygen and transform the substrate to an excited state.
		that is an oxygenase that acts on a substrate luciferin [a bioluminescence substrate] in the presence of molecular oxygen and transforms the substrate to an excited state, which upon return to a lower energy level releases the energy in the form of light.
		Thus, for purposes herein bioluminescence encompasses light produced by reactions that are catalyzed by [in the case of luciferases that act enzymatically] or initiated by [in the case of the photoproteins, such as aequorin, that are not regenerated in the reaction] a biological protein or analog, derivative or mutant thereof.
	www.wipo.int /cgi-pct/guest/getbykey5?KEY=98/26277.981119&ELEMENT_SET=DECL (8716 words)

	[No title] (Site not responding. Last check: 2007-11-06)
		ATP, luciferin (D-luciferin cofactor), luciferase (enzyme) and oxygen are reacted in the presence of magnesium ion.
		Luciferin and luciferase are the same cofactor and enzyme present in fireflies that yields their namesake light.
		Typically, the luciferase, luciferin, and magnesium ion are sold as a single combined reagent, not as individual reagents.
	www.wipo.int /cgi-pct/guest/getbykey5?KEY=98/37229.980827&ELEMENT_SET=DECL (7210 words)

	Luciferin: D-Luciferin Potassium Salt: Luciferase: Biophotonic Imaging: In Vivo, In Vitro Protocols: Tumor Models: IVIS ...
		Luciferin is a low molecular weight organic compound that consists of a benzothiazole moiety attached to a thiazole carboxylic acid moiety.
		Luciferin is found in fireflies and other animals which, in the presence of ATP and the enzyme luciferase, becomes luminescent.
		Luciferin is able to pass the blood brain barrier, the blood placenta barrier and the blood testis barrier, toxicity appears low.
	www.xenogen.com /wt/page/luciferin (397 words)

	Anemaw [Animal Electromagnetism and Waves] : Bioluminescence . © Elizabeth Gerrow 2002 .
		Luciferin, believed to exist in six types as organisms use different forms of luciferin, is a light emitting compound which may be acquired by an organism through internal synthesis or externally through diet (22).
		Luciferin may be stored under an area of transparent cuticle in the light organ, where a layer of dense tissue may be found behind the luciferin, acting as a reflector.
		In order to produce light in the chemical reaction, luciferin must be oxidized with the aid of the natural enzyme, luciferase, an oxygenase (adds oxygen to compounds) which requires a substrate (luciferin) and oxygen (also may require salt) to excite electrons to make them transfer to a higher energy orbital.
	members.fortunecity.com /anemaw/bioluminescence.htm (996 words)

	From the Top of the World...
		Luciferase is an enzyme that catalyzes the oxidation of luciferin.
		Luciferin and luciferase occur in the salivary gland found below the sea firefly's lower jaw.
		Luciferin and luciferase are released into the sea water as granules.
	www.bigelow.org /foodweb/microbe4.html (818 words)

	ISBC - International Society for Bioluminescence and Chemiluminescence
		Bioluminescence involves the oxidation of a substrate (luciferin) in the presence of an enzyme (luciferase).
		This compound is known as coelenterazine because it was first identified in jellyfish (coelenterates) and its molecular structure is derived from a ring of 3 amino-acids (2 tyrosines, and a phenyl alanine).
		The luciferin of Vargula (previously named Cypridina) was the first to be identified and is a tripeptide similar to coelenterazine, but made up of three different amino acids.
	www.isbc.unibo.it /Files/BC_PlanktonNekton.htm (3887 words)

	BL Web: Luciferin types
		Although there are hundreds of types of luminous animals in the sea, there are surprisingly few basic luciferins (light emitters) which have been found in across many species.
		In some cases this conservation can be explained by animals acquiring luciferin through the food chain, but in other cases organisms have been shown to have the ability to synthesize the same chemical on their own.
		Below are examples of the major luciferin types which have been examined, as well as the organisms which use that particular system.
	www.lifesci.ucsb.edu /~biolum/chem/detail1.html (117 words)

	BioMed Central \| Full text \| Optical imaging of luminescence for in vivoquantification of gene electrotransfer in mouse ...
		Lastly addition of luciferin (100 μg/40 μl) to isolated electrotransfered tibial cranial muscle in a multiwell plate induced the same type of decreased kinetics, despite a large excess of substrate and the absence of washout problems.
		In addition, a clear dose effect was observed in vivo 8 days after intramuscular electrotransfer of 0.3, 3 or 30 μg of plasmid, which is consistent with in vitro measurements of this study and confirmed the in vitro results of a previous work [37].
		We verified that addition of ATP with luciferin allowed to obtain luminescence but it is not obvious that in these conditions the luminescence measured would be equivalent to that measured for the same amount of intracellular luciferase.
	www.biomedcentral.com /1472-6750/6/16 (7811 words)

	Visualization of ATP Release in Pancreatic Acini in Response to Cholinergic Stimulus. USE OF FLUORESCENT PROBES AND ...
		Carbachol decreases the luciferin intensity in the acinar lumen.
		The luciferin fluorescence intensity is represented in pseudo-colors, as indicated by the bar.
		The decreases in the fluorescence intensity with CCH indicate appearance of released ATP in the bath and possibly the lumen.
	www.jbc.org /cgi/content/full/276/35/32925 (5466 words)

	Firefly, HYG-2125-95
		The firefly contains luciferin and luciferase, two rare chemicals used in research on cancer, multiple sclerosis, cystic fibrosis and heart disease.
		Nearly 100 percent of the energy is given off as light; in an electric arc light, only 10 percent of the energy is light and the other 90 percent is given off as heat.
		Luciferin, a heat resistant substrate, is the source of light; luciferase, an enzyme, is the trigger; and oxygen is the fuel.
	ohioline.osu.edu /hyg-fact/2000/2125.html (954 words)

	Luciferin - TheBestLinks.com - Adenosine triphosphate, Bacteria, Chlorophyll, Energy, ... (Site not responding. Last check: 2007-11-06)
		Luciferin is a pigment found in organisms capable of bioluminescence, like fireflies, deep sea fish and microbes.
		Bacterial luciferin - riboflavin phosphate - found in bacteria, and some squids and fish
		Dinoflagellate luciferin - a chlorophyll derivitave - found in dinoflaggelates (a type of marine plankton) and euphesiid shrimp
	www.thebestlinks.com /Luciferin.html (171 words)

	Hastings Lab Publications
		Mittag, M., Lee, D.-H., Hastings, J.W. (1994) Circadian expression of the luciferin binding protein correlates with the binding of a protein to its 3' untranslated region.
		Morse, D., Pappenheimer, A.M and Hastings, J.W. (1989) Role of a luciferin binding protein in the circadian bioluminescent reaction of G.
		Dunlap, and Hastings, J.W. (1981) Biochemistry of dinoflagellate bioluminescence: The purification and characterization of dinoflagellate luciferin from Pyrocystis lunula.
	www.mcb.harvard.edu /hastings/Images/JWHPublications.html (7960 words)

	[No title]
		Luciferin: I work in one of those giant office buildings on the river Reechard: lol, I don't have to go that far Luciferin: well...it's also close to FIT...that's the main reason for moving there....you work at Harris right?
		Luciferin: well....we get the place on the 1st of August...so...any time after that Reechard: thats cool Luciferin: yeah...it gives me about 3 weeks to get settled in before school starts again Reechard: yeah.
		Pushy and controlling Luciferin: well....as long as 1) your sister can pay rent 2) you can stand her 3) and she's pretty decent to live with then I have no problems with her having the other room Reechard: cool * Luciferin** signed off at Thu Jul 18 19:34:40 2002.
	home.cfl.rr.com /reechard/David.txt (1035 words)

	BL Web: Chemistry Details
		In the genus Gonyaulax, at pH 8 the molecule is "protected" from the luciferase by a "luciferin-binding protein", but when the pH lowers to around 6, the free luciferin reacts and light is produced.
		A modified form of this luciferin is also found in herbivorous euphausiid shrimp, perhaps indicating a dietary link for the acquisition of luciferin.
		is the most "popular" of the marine luciferins, found in a variety of phyla.
	www.lifesci.ucsb.edu /~biolum/chem/detail2.html (233 words)

	Bioluminescence in Fireflies
		The idea is to use the heat from the water to destroy all the luciferase enzyme leaving only luciferin which is not destroyed by heat.
		No more than a minute or two of heat exposure should be required to destroy all the enzyme; the exact amount of time depends upon the amount of fireflies you are processing and the initial temperature of the water.
		When the lanterns are no longer glowing you know all the luciferase has been destroyed and you may return the luciferin extract to room temperature.
	www.byteland.org /naturalist/dubois.htm (1027 words)

	Krill - Wikipedia, the free encyclopedia
		Except for the Bentheuphausia amblyops species, krill are bioluminescent animals having organs called photophores that are able to emit light.
		The light is generated by an enzyme-catalyzed chemoluminescence reaction, wherein a luciferin (a kind of pigment) is activated by a luciferase enzyme.
		Studies indicate that the luciferin of many krill species is a fluorescent tetrapyrrole similar but not identical to dinoflagellate luciferin
	en.wikipedia.org /wiki/Krill (3410 words)

	BiolumChemicals (Site not responding. Last check: 2007-11-06)
		One common characteristic of the molecules, regardless of organism, is that the main chemical for bioluminescence is luciferin.
		Bacterial luciferin is the luciferin commonly found in bacteria, some fish, and some squid.
		Bacterial luciferin is different from the other luciferins in that it is more of a straight chain molecule.
	www.sas.upenn.edu /~santelli/BiolumChemicals.html (196 words)

	My Science Project
		Several general luciferins are found within a variety of species.
		Via the lux operon, bioluminescence is made useful in uncovering hidden elements, bacteria, and genetic processes otherwise unknown to exist in an environment.
		During bioluminescence, luciferin and luciferase are released by the cells.
	www.midthun.net /newpage11.htm (3715 words)

	Bioluminescent Detection of Endotoxin Effects on HIV-1 LTR-driven Transcription in Vivo -- Yull et al. 51 (6): 741 -- ...
		For each time point, 1 mg of luciferin was administered as an IP injection and bioluminescence was measured 30 min later in the supine position.
		Three mice were treated with 1 mg, 3 mg, or 6 mg of IP luciferin and bioluminescence was measured at baseline (BL) and 4 hr after a single IP dose of 3 µg/g of LPS.
		Luciferin was injected IP at a dose of 3
	www.jhc.org /cgi/content/full/51/6/741 (4067 words)

	Firefly Flashes and NO
		The photocyte mitochondria are found in the peripheral cytoplasm, concentrated especially at locations proximal to the trachea and tracheoles.
		Luciferin is activated by luciferase in an ATP-dependent step to form a luciferin-adenylyl intermediate; when oxygen is present this intermediate is rapidly converted to a peroxyluciferin product that decays to oxyluciferin with the emission of photons.
		In quiescent mode (above dotted line), oxygen delivered through lantern tracheae is consumed by respiration in photocyte mitochondria (green) clustered in the peripheral cytoplasm: little oxygen reaches peroxisomes that contain the light-producing reactions of the luciferin-luciferase pathway.
	ideaplace.org /Why/FireflyFlashEtc.html (434 words)

	Rapid Film-Based Determination of Antibiotic Susceptibilities of Mycobacterium tuberculosis Strains by Using a ...
		A total of 20 µl of phAE85 was added to each sample, and after a further 6-h incubation, 100 µl of flash luciferin buffer was added and the plate was loaded in the Bronx Box for a 12-h exposure.
		CFU (right) were each treated with 100 µl of glow luciferin buffer (see text), loaded in the Bronx Box, and exposed for 3 h.
		The mycobacteria were then treated with 100 µl of glow luciferin buffer, loaded in the Bronx Box, and exposed for 3 h.
	jcm.asm.org /cgi/content/full/37/4/1144 (4714 words)

	Chemical & Engineering News: Science & Technology-All That Glows
		Instead, they use a luciferin of intrinsically higher energy and prepackage it with oxygen in an enzyme known as a photoprotein.
		Steven Haddock, a marine biologist with the Monterey Bay Aquarium Research Institute, Moss Landing, Calif., recently came upon a new twist in the use of bioluminescence in the ocean.
		One possibility is that organisms obtain their luciferin through diet.
	pubs.acs.org /cen/science/84/8414biolum.html (1475 words)

	Jack's "Bugs in the News" - What the Heck is a Bug Light, Please?
		The kind (color) of light depends on the kind of luciferase enzyme (a little different reaction between oxygen, and luciferin among different organisms, and indeed, even within the same organism), and the amount of oxidation of the vitamin attached to luciferin which ultimately occurs.
		Luciferin will enter the cells and float around inside.
		Therefore, in the presence of luciferin, the enzyme luciferase, and molecular oxygen, the bacterial cells which have a working Hooray!
	people.ku.edu /~jbrown/light.html (879 words)

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