Fluorescent Proteins: Aequorin and Luciferase University of Georgia Research Foundation

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Fluorescent Proteins: Aequorin And Luciferase University of Georgia Research Foundation Bioluminescent animals possess special enzymes, pigments and other compounds that, when present in sufficient concentrations, can produce flashes of dazzling blue and green light that they use to communicate, attract mates, distract predators or lure unsuspecting prey. Many researchers imagined using the naturally glowing substance to track important processes in the human body, harnessing the proteins for medical research, diagnostics and therapeutics. But the only reliable sources for the light- emitting substances were the animals themselves, making them both difficult to acquire and prohibitively expensive. A group of scientists from the University of Georgia tackled this problem by studying light- emitting proteins harvested from Renilla and Aequorea, better known as the sea pansy and crystal jellyfish. After years of experimentation, Milton Cormier, Douglas Prasher, Richard McCann and William Lorenz found a way to produce two proteins–Aequorin and Luciferase–using E. coli. Their discoveries enabled the industrial-scale production of these critical proteins, and now, less than 30 years later, bioluminescent proteins are used in many branches of medicine and industry. They serve as indicators for reporter genes, a kind of tag used to see the expression of certain genes in an organism. Their fluorescent glow makes it possible to trace infections, cancer progression, brain function and the development of nerve cells. Bioluminescent proteins are also used to evaluate the effectiveness of new cancer treatments designed to limit blood flow to tumors. The scientists did their work during the 1980s, well before the aid of the now ubiquitous computational and robotic tools, as part of UGA’s newly formed department of biochemistry and molecular biology. Aequorin is cited in nearly 3,800 U.S. patents, and luciferase in 2,000. To see available technologies from research institutions, click here to visit the AUTM Innovation Marketplace. Share your story at autm.net/betterworldproject #betterworldproject.

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Acidic Phospholipids,47, 58 Acidification Steps, 23 Adsorbent, 53
Index acidic phospholipids,47, 58 ATPase, 22, 107 acidification steps, 23 auto-oxidation, 48,49 adsorbent, 53 aequorin, 95 aggregated mitochondria, 23 bacterial cells, 10 alcohols, 49 bacteriorhodopsin (BR), 218,232 alkaline hydrolysis, I bee venom, 121 alkyl esters, 57, 59 binders,53 amide bond, 129 silica gel, 53, 65, 176 amide linkage, 14 silica gel H, 176 amino alcohol, II bioactive phospholipids, 144 amino-group labelling reagents, 121 blanching, 50 aminopeptidase, 17 buoyant density, 16 aminophospholipid, 113, 118 butyl hydroxy toluene (BHT), 49,212 aminophospholipid pump, 119, 140 aminophospholipid translocase, 11 3 amphotericin B (AmB), 107 Cal+ -ATPases, 28, 107 N-(1-deoxyD-fructos-1-yl) AmB, 107 Cal+ -uptake, 27 anchored lipids, 38 campesterol, 104 angular amplitude, 89 calciferol, 78 anilino-8-naphthalene sulfonate (ANS), Candida albicans, 59, 60, 61, 76, 78, 102, 94, 103 104, 108 animal cells, 10 caproic acid, 129, 130 animal tissues, 9 carotenoids, 37 anion transporter, 135 cell debris, 33 anisotropy, 81 , 89, 95, 96, 97, 102, 104, cell disintegrator, 19 105 ceramide, 14, 129, 194 antagonists, 178 ceramide monohexosides ( CMH), 60 antioxidant, 49, 50 cerebroside, 14 apolar lipids, 56, 57, 69 chemical probes,112 arachidonic acid (AA), 144,153, 161 chloroplast, 32, 33 artificial membrane, 83 isolation, 32, 33 ascending chromatography, 54 purification, 33 asymmetric topology, 128 cholesterol, 14, 15,212 asymmetry, 112, 113,119 choline, 7, 9 atebrin, 95 chromatograms, 55 Index 249 chromatographic analyses, 52 ELISA, 146, 148
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