[Bioluminescent method of determining picomolar amounts of nicotinamide-adenine dinucleotide using an immobilized extract of the luminescent bacterium Beneckea harveyi]. 1985

O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis

The luminous bacteria Beneckea Harveyi were immobilized on BrCN-sepharose and cellulose films activated with cyanuric chloride. Preparations with high luciferase and FMN-reductase activities were obtained, which showed no background luminescence without NADH being added. The storage conditions for the preparations obtained were optimized, and their kinetic parameters and thermostability were studied. Standard curves for NADH determining within the concentration range 1 nM-1 microM were plotted with the detection level of 1 picomol NADH. The preparations are very promising for bioluminescent assay due to their high activity, simple production, high stability during storage and a possibility for the repeated use.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008156 Luciferases Enzymes that oxidize certain LUMINESCENT AGENTS to emit light (PHYSICAL LUMINESCENCE). The luciferases from different organisms have evolved differently so have different structures and substrates. Luciferase
D008163 Luminescent Measurements Techniques used for determining the values of photometric parameters of light resulting from LUMINESCENCE. Bioluminescence Measurements,Bioluminescent Assays,Bioluminescent Measurements,Chemiluminescence Measurements,Chemiluminescent Assays,Chemiluminescent Measurements,Chemoluminescence Measurements,Luminescence Measurements,Luminescent Assays,Luminescent Techniques,Phosphorescence Measurements,Phosphorescent Assays,Phosphorescent Measurements,Assay, Bioluminescent,Assay, Chemiluminescent,Assay, Luminescent,Assay, Phosphorescent,Assays, Bioluminescent,Assays, Chemiluminescent,Assays, Luminescent,Assays, Phosphorescent,Bioluminescence Measurement,Bioluminescent Assay,Bioluminescent Measurement,Chemiluminescence Measurement,Chemiluminescent Assay,Chemiluminescent Measurement,Chemoluminescence Measurement,Luminescence Measurement,Luminescent Assay,Luminescent Measurement,Luminescent Technique,Measurement, Bioluminescence,Measurement, Bioluminescent,Measurement, Chemiluminescence,Measurement, Chemiluminescent,Measurement, Chemoluminescence,Measurement, Luminescence,Measurement, Luminescent,Measurement, Phosphorescence,Measurement, Phosphorescent,Measurements, Bioluminescence,Measurements, Bioluminescent,Measurements, Chemiluminescence,Measurements, Chemiluminescent,Measurements, Chemoluminescence,Measurements, Luminescence,Measurements, Luminescent,Measurements, Phosphorescence,Measurements, Phosphorescent,Phosphorescence Measurement,Phosphorescent Assay,Phosphorescent Measurement,Technique, Luminescent,Techniques, Luminescent
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009247 NADH, NADPH Oxidoreductases A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6. Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D001681 Biological Assay A method of measuring the effects of a biologically active substance using an intermediate in vivo or in vitro tissue or cell model under controlled conditions. It includes virulence studies in animal fetuses in utero, mouse convulsion bioassay of insulin, quantitation of tumor-initiator systems in mouse skin, calculation of potentiating effects of a hormonal factor in an isolated strip of contracting stomach muscle, etc. Bioassay,Assay, Biological,Assays, Biological,Biologic Assay,Biologic Assays,Assay, Biologic,Assays, Biologic,Bioassays,Biological Assays
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures
D014733 Vibrio A genus of VIBRIONACEAE, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle. Beneckea
D014737 Vibrionaceae A family of gram-negative bacteria whose members predominate in the bacterial flora of PLANKTON; FISHES; and SEAWATER. Some members are important pathogens for humans and animals.
D038181 FMN Reductase An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29. Flavin Mononucleotide Reductase,NAD(P)H-Flavin Oxidoreductase,FMN Oxidoreductase,NAD(P)H Dehydrogenase (FMN),NAD(P)H-FMN Oxidoreductase,NADH-FMN Oxidoreductase,NADH-Flavin Oxidoreductase,NADPH-Flavin Reductase,Mononucleotide Reductase, Flavin,NADH FMN Oxidoreductase,NADPH Flavin Reductase,Oxidoreductase, FMN,Oxidoreductase, NADH-FMN,Oxidoreductase, NADH-Flavin,Reductase, FMN,Reductase, Flavin Mononucleotide,Reductase, NADPH-Flavin

Related Publications

O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
January 1978, The Journal of biological chemistry,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
January 1977, The Italian journal of biochemistry,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
December 1973, The Biochemical journal,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
June 1978, Canadian journal of biochemistry,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
February 1979, Journal of bacteriology,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
November 1993, Archives of biochemistry and biophysics,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
November 1962, Plant physiology,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
January 1997, Biotechnology and bioengineering,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
January 1986, Methods in enzymology,
O V Lebedeva, and N N Ugarova, and T V Deĭko, and E I Raĭnina, and T A Makhlis
June 1998, Analytical biochemistry,
Copied contents to your clipboard!