Acidic Phospholipids,47, 58 Acidification Steps, 23 Adsorbent, 53

Total Page:16

File Type:pdf, Size:1020Kb

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 chromatoplate, 54, 55, 57 emission anisotropy, 95 complex lipids, 11, 50 energy transfer parameter (E), 98 Con A modified spheroplasts, 24 enzymatic probes, 112,119 Coryphenoides armatus, 105 eosin,95 Coryphenoides rupestris, 105 equilibrium density, 16, 18 critical micellar concentration (CMC), ergosterol, 14, 15, 77,78 210, 211 erythrocyte membrane, 10,119 crude membrane, 18, 22 ESR (electron spin resonance), 80, 81, 83, cyclic AMP, 168 86, 87,90 cytochrome C oxidase, 17 essential fatty acids (EFA), 106 estimation of inorganic phosphate, 127 ethanolamine, 9 dansyl chloride (DNS-Cl), 94 evaporation, 44,47 deacylase-reacylase repairing system, extraction of sterols, 74 129 DEGS,69, 70 density gradient centrifugation, 18 fatty acids,10, 11, 57 CsCl-density centrifugation, 34 melting point, 3 discontinuous gradient, 31 ficoll,31 depolarization, 96 Flame Ionisation Detector (FID), 70,78 diacylglycerol, 11, 57, 59,76 fluidity, 203, 213 diacylglycerophospholipid, 121,127 fluorescamine, 116 dielectric constant, 50 fluorescein5'-isothiocyanate (FITC), 94 diffusion coefficient, 96 fluorescence,93,96,104, 133 digalactosyldiacylglycerols, 11 fluorescence anisotropy, 95, 96, 101, 102 dimyristoyl glycerol, 196 fluorescence polarisation measurements, dioleoylphosphatidylethanolamine 105 (DOPE), 106 fluorescence quenching (FQ), 94, 98, 104 dipalmitoylphosphatidylcholine fluorescent analogues,128, 130 (DPPC), 86, 87, 90,101, 106 fluorescent probes, 122,242 dipalmitoyldiglyceride, 197 fluorophores,94, 104 diphosphatidylglycerol (DPG), 2, 9, 11 Forster-type resonance energy transfer DNA dependent RNA polymerase, 17 (FRET), 107 dodecanoic acid, 129, 130 DPH, (all-trans-1,6- diphenyll ,3,5hexatriene) G proteins, 167 94, 101, 102 103 Gaffney's method, 90 TMA-DPH, 105, 107 galactosyldiacylglycerols, 11,12 gangliosides,41, 47 gas liquid chromatography (GLC), 44, 66, egg phosphatidylcholine (EPC), 215, 70,72 220 columns of, 73 egg-phosphatidic acid, 213 GDPase, 17 eicosanoids, 144, 146, 148, 157 gel exclusion chromatography, 229, 230 electrostatic repulsion,213 general tests of lipid detection, 57 250 Index iodine vapour, 59, 62, 175, 178 lipid extraction, 137 sulphuric acid charring, 62 lipid peroxidation, 49 glucocerebroside, 14 lipid-protein complexes, 90 glycerol, 7 lipids, 1, 3, 5, 50 glycerolipids, 212 composition, 1 glycerophospholipid, 121, 129 microbial, 10 glycolipids, 38, 56, 60, 62, 212 mitochondrial membrane, 11 glycosidic bonds, 38 neutral lipids, 60, 61, 63, glycosyldiacylglycerol ,12 non-saponifiable, 1 glycosylphosphatidylinositol, 196, 199 polar lipids, 57 growth factors, 167 saponifiable, 1, 3 GTP binding proteins, 167 lipoamino acid, 10 liposome preparation, 214,219 liposomes, 101,202 H+ -ATPase, 22 giant liposomes, 203, 218 haemolysed cells, 124 large liposomes (LUV), 203 Helix pomatia, 28 large unilamellar vesicles (LUV), 226 high performance liquid multi lamellar vesicles (MLV), 219, chromatography (HPLC), 44, 52, 222 146, 157 small unilamellar vesicles (SUV), hydroxyeicosatetraenoic acids 222,223 (HETES), 145, 146 unilamellar vesicles, 100,222 hyperfine splitting, 89 very large unilamellar vesicles (VLUV), 204,219,228 lipoxins, 145 inner monolayer, 119 lipoxygenases, 145 inositol, 9, 10 liquid partition chromatography, 48 inositol phosphateglycan, 196 lyophilisation, 212 inositol polyphosphate phosphatase., lysophospholipids, 41, 121 170 inositolphosphates, 170, 178, 186 interleukins, 193,196 mannoproteins, 24 intramolecular fluorescence energy marker enzymes, 17 transfer (IFET), 98, 100, 107 Mcilwain tissue chopper, 179 isopycnic centrifugation, 16 membrane bound enzymes, 167 membrane lipid extraction, 39 membrane protein reconstitution,231 labelled fatty acids, 130 membrane spin labels, 88 lanosterol, 77 methanolysis, 66 lateral mobility, 213 methyl esters, 66, 67 lectin,24 micro viscosity, 95 lukotrienes,(LTs), 145,146, 158,159, mitochondrial lipids, 11, 101 161,162, 159 monoacylglycerols, 57 lipases, 41 monoenoic fatty acids, 3 lipid analysis, 48 monogalactosyldiacylglycerols, 11 lipid bilayer, 95 monoxygenase, 145 Index 251 Naja naja, 121 derivative, 10 NBD,129, 130 mono- and di-methyl-, 10 ninhydrin test, 63 phosphatidylglycerol (PG),2, 9, 10, nitroxide radical, 134 11,60, 61 non-lipid contaminants, 47 phosphatidylinositides (Pis), 10, 61, non-permeant probes, 114 121, 171,174 nonpolar solvents, 39 phosphatidylinositol-4,5-bisphosphate NADPH Cytochrome C oxidoreductase, (PIP), 168,170,174,176 17 phosph~tidylinositol-4-phosphate (PIP),168, 170,174,178 phosphatidyl serine (PS), 10,61,121,128, 175 octyl [3-D-glucopyranoside, 228, 240 phosphodiester bridges, 11 oleic acid, 3 phosphoglyceride,5, 6, 38 order parameter, 96, 98 phospholipase A2, 120, 121, 122, 123, organelle lysis, 139 144 osmotic gradient, 215 phospholipase C, 120, 196, 197 phospholipase D, 130,189, 190 phospholipid, 5,6,9 palmitic acid, 3 analysis, 117, 126 paramagnetic analogues, 128,133 asymmetry, 119 paramagnetic probes, 128 distribution, 119, 121 partition coefficient, 93 exchange protein, 122 PCSL (1-acyl-2-(n-(4,4- phosphoric acid, 6 dimethyloxazolidine-N­ phosphorescence, 106 oxy)stearoy I)-sn-gl yc ero-3- phosphorylcholine, 14,194 phosphocholine), 86 phosphorylethanolamine, 14 pentanoic acid, 129 photosynthetic reduction, 34 perhydrocyclopentanophenanthrene, 15 plant tissues, 9, 41 peroxidised phospholipids, 129 plasma membrane(PM), 24, 102 Perrin equation, 95 isolation, by mechanical disruption, PG (prostaglandins) measurement, 19 145,146 isolation of yeast,20 phase transition, 80, 81 ,.83 polar head group, 6, 210 phenylmethylsulphonyl fluoride, polar lipids,38, 52, 57,60 (PMSF), 30 polar solvent, 39 phosphatidic acid, 190 polarity, SO, 51 phosphatases, 167 polarization, 95 phosphatides, 5 polyenoic, 3 phosphatidylcholine, (PC),7, 9, polyphosphoinositides, 10, 41, 58, 170 63,113,120,190 polyunsaturated fatty acids, 3, 171 phosphatidylcholine signal pathway, porcine pancreas, 121 189 prostacyclin, 153 phosphatidylethanolamine (PE), 7, 9, prostaglandins (PG), 148, 153 63, 113, 121 protease inhibitors, 20 lyso-derivative, 9 protein kinases, 167 252 Index protein kinase C, 168, 190 spheroplasts, 20 protein secretory pathway, 25 sphingolipid signal pathway; 193 proteoliposomes, 231, 242 sphingolipids, 5, 11, 212 protonophore, 27 sphingomyelin (SM), 2, 13, 122, 128 protoplast, 41,87 sphingomyelinase, 122, 194 pseudofluorescence anisotropy decay, sphingomyelinase C, 122, 124 96 sphingosine, 5, 11, 14 proteases A, B, 17 sphingosylphosphocholine moiety, 130 spin labelled lipid, 81 squalene, 77, 78 radioimmunoassay (RIA), 146 Staphylococcus aureus, 121 RBC membrane, 40 steady-state fluorescence anisotropy resonance absorption, 81 (SSFA), 95, 104 restriction endonucleases, 34 stearic acid, 3 R, values, 54 sterols, 14, 15, 37, 57, 74,95 rotational correlation time ('tR), 91 steryl esters, 57, 77 rotational diffusion, 80 stigmasterol, 104 rotational mobility, 85 storage of lipids, 48 rotational relaxations, 106 subcellular membranes, 17 reverse phase HPLC, 159 sucrose density gradient,27 sulfolipids, 11 sulphonic acid, 11 SASL (n-( 4,4-dimethyloxawlidine-N- surfactant solubilization, 205 oxy) stearic acid), 85, 90 suspension buffer, 17 S-p space, 16, 18 synthetic phospholipids,212 S. cerevisiae, 25 saponifiable lipids, 1, 3, temperaturesensitive mutants, 25 saturated fatty acids 3, 4 TG, (triacylglycerols), 49,57 saturated lipids, 62 THF, 101 second messenger, 167 thin layer chromatography, (TLC),44, sedimentation rate, 16 52, 117 sedimentation coeffiecient, 18 thromboxane (Tx), 145, 146 seminaphoto- r hodafluor-1- transition temperature, 83, 207 acetoxymethylester (SNARF-1-AM), translational diffusion, 81 94, 108 transmembrane distribution, 128 sickle RBC, 113 TRFA, 96,105 signal amplitude, 88 trinitrobenzene sulfonic acid ( TNBS ), signal reduction, 135 114, 115, 118 signal transduction, 167, 194 trinitrophenylatedPE (TNP-PE), 114 sitosterol, 104 tumour necrosis factor' (TNF-'), 193 snail enzyme or lyticase, 21,31 two - dimensional
Recommended publications
  • Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents
    International Journal of Molecular Sciences Article Bioluminescent Properties of Semi-Synthetic Obelin and Aequorin Activated by Coelenterazine Analogues with Modifications of C-2, C-6, and C-8 Substituents 1, 2,3, 1 2, Elena V. Eremeeva y , Tianyu Jiang y , Natalia P. Malikova , Minyong Li * and Eugene S. Vysotski 1,* 1 Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk 660036, Russia; [email protected] (E.V.E.); [email protected] (N.P.M.) 2 Key Laboratory of Chemical Biology (MOE), Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan 250012, China; [email protected] 3 State Key Laboratory of Microbial Technology, Shandong University–Helmholtz Institute of Biotechnology, Shandong University, Qingdao 266237, China * Correspondence: [email protected] (M.L.); [email protected] (E.S.V.); Tel.: +86-531-8838-2076 (M.L.); +7-(391)-249-44-30 (E.S.V.); Fax: +86-531-8838-2076 (M.L.); +7-(391)-290-54-90 (E.S.V.) These authors contributed equally to this work. y Received: 23 June 2020; Accepted: 27 July 2020; Published: 30 July 2020 Abstract: Ca2+-regulated photoproteins responsible for bioluminescence of a variety of marine organisms are single-chain globular proteins within the inner cavity of which the oxygenated coelenterazine, 2-hydroperoxycoelenterazine, is tightly bound. Alongside with native coelenterazine, photoproteins can also use its synthetic analogues as substrates to produce flash-type bioluminescence. However, information on the effect of modifications of various groups of coelenterazine and amino acid environment of the protein active site on the bioluminescent properties of the corresponding semi-synthetic photoproteins is fragmentary and often controversial.
    [Show full text]
  • Bioluminescence Related Publications from JNC Corporation
    Bioluminescence related publications since 1985 110) Inouye, S. and Hojo, H. (2018) Revalidation of recombinant aequorin as a light emission standard: Estimation of specific activity of Gaussia luciferase. Biochem. Biophys. Res. Commun. 507: 242-245. 109) Yokawa, S., Suzuki, T., Hayashi, A., Inouye, S., Inoh, Y. and Furuno, T. (2018) Video-rate bioluminescence imaging of degranulation of mast cells attached to the extracellular matrix. Front. Cell Dev. Biol. 6: 74. 108) Inouye, S., Tomabechi, Y., Hosoya, T., Sekine, S. and Shirouzu, M. (2018) Slow luminescence kinetics of semi-synthetic aequorin:expression, purification and structure determination of cf3-aequorin. J. Biochem. 164(3): 247–255. 107) Inouye, S. (2018) Single-step purification of recombinant Gaussia luciferase from serum-containing culture medium of mammalian cells. Protein Expr. Purif. 141: 32-38. 106) Inouye, S. and Sahara-Miura, Y. (2017) A fusion protein of the synthetic IgG-binding domain and aequorin: Expression and purification from E. coli cells and its application. Protein Expr. Purif. 137: 58-63. 105) Suzuki, T., Kanamori, T. and Inouye, S. (2017) Quantitative visualization of synchronized insulin secretion from 3D-cultured cells. Biochem. Biophys. Res. Commun. 486: 886-892. 104) Yokawa, S., Suzuki, T., Inouye, S., Inoh, Y., Suzuki, R., Kanamori, T., Furuno, T. and Hirashima, N. (2017) Visualization of glucagon secretion from pancreatic α cells by bioluminescence video microscopy: Identification of secretion sites in the intercellular contact regions. Biochem. Biophys. Res. Commun. 485: 725-730. 103) Inouye, S. and Suzuki, T. (2016) Protein expression of preferred human codon-optimized Gaussia luciferase genes with an artificial open-reading frame in mammalian and bacterial cells.
    [Show full text]
  • BPS Complete Catalog
    BPSCATALOG ENZYMES KITS CELL LINES SCREENING SERVICES INNOVATIVE PRODUCTS TO FUEL YOUR EXPERIMENTS Unique, expert portfolio 2017 OUR MISSION: To provide the highest quality life science products and services worldwide in a timely manner to assist in accelerating drug discovery research and development for the treatment of human diseases. INNOVATION WE CONTINUOUSLY STRIVE TO BE FIRST TO MARKET BY PROVIDING EXPERTISE IN EXPRESSING HIGHLY ACTIVE ENZYMES MULTIPLE ASSAY DETECTION FORMATS HUMAN, MURINE AND MONKEY VERSIONS OF RECOMBINANT PROTEINS BIOTINYLATED VERSIONS OF MANY IMMUNE CHECKPOINT RECEPTORS 1ST AND MOST EXTENSIVE PARP ISOZYME PORTFOLIO 1ST AND MOST EXTENSIVE PDE ISOZYME PORTFOLIO 1ST COMPLETE SUITE OF HDAC AND SIRT ENZYMES 1ST AVAILABLE PARP AND TANKYRASE PROFILING SERVICES 1ST COMMERCIALLY AVAILABLE HISTONE DEMETHYLASES LARGEST OFFERING OF METHYLTRANSFERASES LARGEST OFFERING OF DEMETHYLASES OVER 200 PRODUCTS AND SERVICES EXCLUSIVE TO BPS RELIABILITY BPS IS CITED IN PEER-REVIEWED JOURNALS AND PUBLICATIONS AROUND THE WORLD NATURE GENETICS THE JOURNAL OF BIOLOGICAL CHEMISTRY JOURNAL OF CELL SCIENCE ANALYTICAL BIOCHEMISTRY BBRC NATURE CHEMICAL BIOLOGY ACS MEDICINAL CHEMISTRY LETTERS JOURNAL OF NATURAL PRODUCTS CHEMMEDCHEM MOLECULAR CANCER THERAPEUTICS & MANY MORE TABLE OF CONTENTS ACETYLTRANSFERASE 4 APOPTOSIS 4-5 ANTIBODIES 6-9 BIOTINYLATION 10-11 BROMODOMAINS 12-14 CELL BASED ASSAY KITS 15 CELL LINES 16-17 CELL SURFACE RECEPTORS 18-20 CYTOKINE(S) 21-24 DEACETYLASE(S) 25-27 DEMETHYLASE(S) 28-29 HEAT SHOCK PROTEINS 30 IMMUNOTHERAPY
    [Show full text]
  • Platelet-Neutrophil Interaction
    PLATELET-NEUTROPHIL INTERACTION: NEUTROPHILS MODULATE PLATELET FUNCTION Richard William FAINT 1992 A thesis submitted to the University of London for the degree of Ph.D The Department of Haematology University College and Middlesex School of Medicine University College London 98 Chenies Mews London WC1E 6HX ProQuest Number: U049250 All rights reserved INFORMATION TO ALL USERS The quality of this reproduction is dependent upon the quality of the copy submitted. In the unlikely event that the author did not send a com plete manuscript and there are missing pages, these will be noted. Also, if material had to be removed, a note will indicate the deletion. uest ProQuest U049250 Published by ProQuest LLC(2017). Copyright of the Dissertation is held by the Author. All rights reserved. This work is protected against unauthorized copying under Title 17, United States C ode Microform Edition © ProQuest LLC. ProQuest LLC. 789 East Eisenhower Parkway P.O. Box 1346 Ann Arbor, Ml 48106- 1346 2 ABSTRACT Platelets are vital for the arrest of bleeding following tissue injury. Neutrophils play an important role in host defence against bacterial infection. In the milieu of the acute inflammatory response both cellular and non-cellular elements may interact to modify behaviour. Evidence suggests that leukocytes may play an active role in the modulation of platelet function. This interaction may be abnormal in certain pathological states. This study examined the effect of purified neutrophils upon both washed platelets and platelet-rich plasma, as well as in whole blood in vitro. Neutrophils were found to alter platelet behaviour by several mechanisms. These included transcellular metabolism of eicosanoids.
    [Show full text]
  • Antibody List
    產品編號 產品名稱 PA569955 1110059E24Rik Polyclonal Antibody PA569956 1110059E24Rik Polyclonal Antibody PA570131 1190002N15Rik Polyclonal Antibody 01-1234-42 123count eBeads Counting Beads MA512242 14.3.3 Pan Monoclonal Antibody (CG15) LFMA0074 14-3-3 beta Monoclonal Antibody (60C10) LFPA0077 14-3-3 beta Polyclonal Antibody PA137002 14-3-3 beta Polyclonal Antibody PA14647 14-3-3 beta Polyclonal Antibody PA515477 14-3-3 beta Polyclonal Antibody PA517425 14-3-3 beta Polyclonal Antibody PA522264 14-3-3 beta Polyclonal Antibody PA529689 14-3-3 beta Polyclonal Antibody MA134561 14-3-3 beta/epsilon/zeta Monoclonal Antibody (3C8) MA125492 14-3-3 beta/zeta Monoclonal Antibody (22-IID8B) MA125665 14-3-3 beta/zeta Monoclonal Antibody (4E2) 702477 14-3-3 delta/zeta Antibody (1H9L19), ABfinity Rabbit Monoclonal 711507 14-3-3 delta/zeta Antibody (1HCLC), ABfinity Rabbit Oligoclonal 702241 14-3-3 epsilon Antibody (5H10L5), ABfinity Rabbit Monoclonal 711273 14-3-3 epsilon Antibody (5HCLC), ABfinity Rabbit Oligoclonal PA517104 14-3-3 epsilon Polyclonal Antibody PA528937 14-3-3 epsilon Polyclonal Antibody PA529773 14-3-3 epsilon Polyclonal Antibody PA575298 14-3-3 eta (Lys81) Polyclonal Antibody MA524792 14-3-3 eta Monoclonal Antibody PA528113 14-3-3 eta Polyclonal Antibody PA529774 14-3-3 eta Polyclonal Antibody PA546811 14-3-3 eta Polyclonal Antibody MA116588 14-3-3 gamma Monoclonal Antibody (HS23) MA116587 14-3-3 gamma Monoclonal Antibody (KC21) PA529690 14-3-3 gamma Polyclonal Antibody PA578233 14-3-3 gamma Polyclonal Antibody 510700 14-3-3 Pan Polyclonal
    [Show full text]
  • Site-Specific Mutagenesis of the Calcium-Binding Photoprotein
    Proc. Natd. Acad. Sci. USA Vol. 83, pp. 8107-8111, November 1986 Biochemistry Site-specific mutagenesis of the calcium-binding photoprotein aequorin (bioluninescence/oxygenase/oligonudeotide-directed mutagenesis/protein modification) FREDERICK I. TsuJI*, SATOSHI INOUYEtt, TOSHIO GOTO§, AND YOSHIYUKI SAKAKIt *Marine Biology Research Division, Scripps Institution of Oceanography, University of California-San Diego, La Jolla, CA 92093, and V. A. Medical Center Brentwood, Los Angeles, CA 90073; tResearch Laboratory for Genetic Information, Kyushu University, Fukuoka 812, Japan; and §Department of Agricultural Chemistry, Faculty of Agriculture, Nagoya University, Nagoya 464, Japan Communicated by Martin D. Kamen, July 21, 1986 ABSTRACT The luminescent protein aequorin from the which amino acid substitutions were made at the three jellyfish Aequoria victoria emits light by an intramolecular Ca2l-binding sites, at the three cysteines, and at histidine in reaction in the presence of a trace amount of Ca2 . In order to the hydrophobic region. understand the mechanism of the reaction, a study of structure-function relationships was undertaken with respect MATERIALS AND METHODS to modifying certain of its amino acid residues. This was done by carrying out oligonudeotide-directed site-specific mutagen- Enzymes and Chemicals. All restriction endonucleases, esis of apoaequorin cDNA and expressing the mutagenized Escherichia coli T4 DNA ligase, Klenow enzyme of DNA cDNA in Escherichia cofi. Amino acid substitutions were made polymerase 1, and T4 polynucleotide kinase were purchased at the three Ca2+-binding sites, the three cysteines, and a from Takara Shuzo (Kyoto, Japan). Tris, 2-mercaptoethanol, histidine in one of the hydrophobic regions. Subsequent assay and isopropyl-,fD-thiogalactopyranoside were obtained from of the modified aequorin showed that the Ca2 -binding sites, Wako Pure Chemicals (Osaka, Japan).
    [Show full text]
  • Chimeric Green Fluorescent Protein-Aequorin As Bioluminescent Ca2؉ Reporters at the Single-Cell Level
    Chimeric green fluorescent protein-aequorin as bioluminescent Ca2؉ reporters at the single-cell level Vale´ rie Baubet*, Herve´ Le Mouellic*, Anthony K. Campbell†, Estelle Lucas-Meunier‡, Philippe Fossier‡, and Philippe Bruˆlet*§ *Unite´d’Embryologie Mole´culaire, Unite´de Recherche Associe´e 1947, Centre National de la Recherche Scientifique, Institut Pasteur, 25 rue du docteur Roux, 75724 Paris Cedex 15, France; †Department of Medical Biochemistry, University of Wales College of Medicine, Heath Park, Cardiff CF4 4XN, United Kingdom; and ‡Laboratoire de Neurobiologie Cellulaire et Mole´culaire, UPR 9040 Centre National de la Recherche Scientifique, avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France Communicated by Franc¸ois Jacob, Institut Pasteur, Paris, France, April 14, 2000 (received for review February 1, 2000) 2ϩ ϭ ␮ Monitoring calcium fluxes in real time could help to understand the Its low affinity for Ca (Kd 10 M) is probably responsible development, the plasticity, and the functioning of the central for this and makes aequorin a good sensor in the range of nervous system. In jellyfish, the chemiluminescent calcium binding biological Ca2ϩ concentration variations. Although providing a aequorin protein is associated with the green fluorescent protein good ratio of signal over background, aequorin signals are very ,and a green bioluminescent signal is emitted upon Ca2؉ stimula- difficult to detect because of aequorin’s low light quantum yield tion. We decided to use this chemiluminescence resonance energy that is the number of emitted photons per protein that bind Ca2ϩ. transfer between the two molecules. Calcium-sensitive biolumi- In the jellyfish Aequorea victoria from which aequorin has been nescent reporter genes have been constructed by fusing green isolated (10), the protein is associated with the GFP (11).
    [Show full text]
  • Chemistry and Control of Luminescence in Marine Organisms
    BULLETIN OF MARINE SCIENCE. 33(4): 818-828, 1983 CHEMISTRY AND CONTROL OF LUMINESCENCE IN MARINE ORGANISMS J. W Hastings ABSTRACT Bioluminescence occurs in very many different marine organisms. The reaction is an enzyme (Iuciferase) mediated chemiluminescence in which a substrate (Iuciferin) is oxidized by molecular oxygen; energy thereby available is conserved in the form of a molecule in an electronically excited (singlet) state which subsequently emits light. The luciferins and lucif- erases utilized in different organisms may be very different, but all known luciferases may be classed as oxygenases, involving peroxides (in some cases ring peroxides) as intermediates; in some cases electron transfer has been postulated in the terminal steps leading to excitation. The cellular control of bioluminescent reactions involves special mechanisms such as the sequestration of substrate by a binding protein or the accumulation ofa reaction intermediate, and a triggering step, as for E:xample by H+ or Ca++, Although bioluminescence is not confined to the marine environment, the pre- ponderance ofluminous species do in fact occur in the sea (Harvey, 1952; Lynch, 1981). Why this is so has had no satisfactory explanation, either in terms of evolutionary or ecological factors, and there appear to be no truly unique biological features of marine luminous systems as such. There also seem to be no important distinctions between marine and nonmarine systems with respect to the chemical reactions responsible for light emission. All are similar in that they involve the oxidation of a substrate by molecular oxygen and result in the formation of a product molecule in an electronically excited state sufficiently energetic to result in the emission of a photon.
    [Show full text]
  • Discovery of Green Fluorescent Protein (GFP) (Nobel Lecture)** Osamu Shimomura*
    Nobel Lectures Angewandte Chemie 5590 www.angewandte.org 2009 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim Angew. Chem. Int. Ed. 2009, 48, 5590 – 5602 Angewandte Green Fluorescent Protein Chemie DOI: 10.1002/anie.200902240 Green Fluorescent Protein Discovery of Green Fluorescent Protein (GFP) (Nobel Lecture)** Osamu Shimomura* aequorin · bioluminescence · fluorescent proteins · Nobel Lecture 1. Biography A Wartime Childhood I was born on August 27, 1928 in the town of Fukuchiyama, Kyoto-Fu, Japan. My father Chikara was an army captain of the Fukuchiyama regiment. In the spring of 1933, my father took a post in Manchuria, which was under Japanese occupation. Because there were some insurgents in the Manchurian area, my mother Yukie, my younger brother Sadamu, and I chose to stay in Japan and moved to Sasebo, Nagasaki Prefecture, where we lived with my grandmother, Tsuki Shimomura. After the insurgents were wiped out, we moved to Renzankan, Manchuria in March 1935. A sister, Toshiko, was born here, but she died of pneumonia one year after her birth. I remember my mothers deep sorrow after Figure 1. Together with my father who returned briefly from Manchuria in 1939. Front row from left: my mother Yukie, grandmother Tsuki, Toshikos death. grandfather Kosaburo, father Chikara, younger brother Sadamu, and In early 1938, my father was transferred to an army myself behind Sadamu, together with my uncle Eijiro Sata’s family in position near the Soviet border. The rest of my family moved the back row. back to Sasebo. Mother soon departed to Manchuria again to live with my father, and Sadamu and I were in the custody of was poor.
    [Show full text]
  • (BRET) for Real Time Detection of Protein-Protein Inte
    University of Tennessee, Knoxville Trace: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 5-2008 Application and Optimization of Bioluminescence Resonance Energy Transfer (BRET) for Real Time Detection of Protein-Protein Interactions in Transgenic Arabidopsis as well as Structure-Based Functional Studies on the Active Site of Coelenterazine-dependent Luciferase from Renilla and its Improvement by Protein Engineering Jongchan Woo University of Tennessee - Knoxville Recommended Citation Woo, Jongchan, "Application and Optimization of Bioluminescence Resonance Energy Transfer (BRET) for Real Time Detection of Protein-Protein Interactions in Transgenic Arabidopsis as well as Structure-Based Functional Studies on the Active Site of Coelenterazine-dependent Luciferase from Renilla and its Improvement by Protein Engineering. " PhD diss., University of Tennessee, 2008. https://trace.tennessee.edu/utk_graddiss/355 This Dissertation is brought to you for free and open access by the Graduate School at Trace: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of Trace: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Jongchan Woo entitled "Application and Optimization of Bioluminescence Resonance Energy Transfer (BRET) for Real Time Detection of Protein-Protein Interactions in Transgenic Arabidopsis as well as Structure-Based Functional Studies on the Active Site of Coelenterazine-dependent Luciferase from Renilla and its Improvement by Protein Engineering." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Plant Sciences.
    [Show full text]
  • Nobel Lecture by Osamu Shimomura
    DISCOVERY OF GREEN FLUORESCENT PROTEIN, GFP Nobel Lecture, December 8, 2008 by Osamu Shimomura Marine Biological Laboratory, Woods Hole, MA 02543, USA. PROLOGUE I discovered the green fluorescent protein GFP from the jellyfish Aequorea aequorea in 1961 as a byproduct of the Ca-sensitive photoprotein aequorin (Shimomura et al., 1962; Johnson et al., 1962), and identified its chro- mophore in 1979 (Shimomura, 1979). GFP was a beautiful protein but it remained useless for the next 30 years after the discovery. My story begins in 1945, the year the city of Nagasaki was destroyed by an atomic bomb and World War II ended. At that time I was a 16-year old high school student, and I was working at a factory about 15 km northeast of Nagasaki. I watched the B-29 that carried the atomic bomb heading toward Nagasaki, then soon I was exposed to a blinding bright flash and a strong pressure wave that were caused by a gigantic explosion. I was lucky to sur- vive the war. In the mess after the war, however, I could not find any school to attend. I idled for 2 years, and then I learned that the pharmacy school of Nagasaki Medical College, which had been completely destroyed by the atomic bomb, was going to open a temporary campus near my home. I ap- plied to the pharmacy school and was accepted. Although I didn’t have any interest in pharmacy, it was the only way that I could have some education. After graduating from the pharmacy school, I worked as a teaching assistant at the same school, which was reorganized as a part of Nagasaki University.
    [Show full text]
  • Assay Kits and Proteins for Drug Discovery
    Assay Kits and Proteins for Drug Discovery PARP UBIQUITINATION EPIGENETICS KINASES PHOSPHATASES Table of Contents Histone & DNA Methylation................................................................................. 2 DNA Methylation................................................................... 2 Assay Kits Components 3 Methylation Enzymes 4 Substrates 5 Inhibitors / Activators 6 Histone Demethylases 6 Demethylase Assay Kits 6 Demethylase Assay Kit Components 7 Demethylase Enzymes 7 Substrates 8 Inhibitors / Activators 8 Histone Acetylation 9 Deacetylase 9 Substrates 9 Deacetylase Assay Kits 9 Deacetylase Enzymes 10 Inhibitors / Activators 11 Histone Acetyltransferases 12 Assay Kits 12 Inhibitors / Activators 12 Enzymes 12 Bromodomains 13 Assay Kits 13 Proteins 13 Ligands 14 Inhibitors / Activators 14 Methyl-Lysine Readers 15 Assay Kits 15 Inhibitors / Activators 15 Proteins 15 PARP 16 Enzymes 16 Assay Kits 16 Inhibitors / Activators 17 Substrates 17 Immunotherapy 18 Antibodies 18 Assay Kits 18 Protein 19 Assay Kit Components 22 Cell Based Assay / Stable Lines 22 Kinase 23 Receptor Tyrosine Kinase 23 Cytoplasmic Tyrosine Kinases 24 Lipid Kinase 25 Serine Threonine Kinase 26 Substrates 29 Inhibitors 30 Cell Based Assay Kits 31 Phosphodiesterase 31 Immunotherapy 31 Cell Signaling Pathways 31 Protein Phosphatases 32 Receptor Tyrosine 32 Non-Receptor 32 Serine 32 Protease 33 Assay Kits 33 Substrates 33 Inhibitors / Activators 33 Enzymes 34 Ubiquitination 35 Activating Enzyme (E1) 35 Conjugating Enzyme (E2) 35 Deubiquitylating Enzymes
    [Show full text]