Results 221 to 230 of about 38,156 (252)

Construction and Characterization of a Novel Direct Electron Transfer Type Enzymatic Sensor Using Spermidine Dehydrogenase. [PDF]

open access: yesBiosensors (Basel)
Tong S   +9 more
europepmc   +1 more source

Pure crystalline flavine adenine dinucleotide

Archives of Biochemistry and Biophysics, 1958
Abstract The preparation of pure, crystalline flavine adenine dinucleotide using electrophoresis on a column packed with cellulose powder followed by chromatography on carboxylic resin is described. The spectra and fluorescence of the pure coenzyme are studied.
P, CERLETTI, N, SILIPRANDI
openaire   +2 more sources

Enzymatic synthesis of flavin adenine dinucleotide

Applied Biochemistry and Biotechnology, 1983
A new and simple enzymatic method for the synthesis of flavin adenine dinucleotide (FAD) from flavin mononucleotide by the transadenylylation reaction using microbial cells is described. Among various microorganisms tested, Artherobacter globiformis IFO 12138 and two soil bacteria were selected as useful enzyme sources.
S, Shimizu   +3 more
openaire   +2 more sources

Flavin adenine dinucleotide synthesis in animal tissues

Biochimica et Biophysica Acta, 1958
Abstract 1. 1. An enzyme which synthesizes flavin adenine dinucleotide (FAD) from flavin mononucleotide (FMN) and adenosine triposphate (ATP) has been localized in the soluble fraction of the cells of animal tissues. This activity has been shown to be widespread; it has been found to be especially high in mouse liver and is found even in skeletal
C, DELUCA, N O, KAPLAN
openaire   +2 more sources

Flavin Adenine Dinucleotide Photophysics in Ice

The Journal of Physical Chemistry C, 2009
Steady-state, time-resolved emission and pump-probe techniques were employed to study the nonradiative process of flavin adenine dinucleotide (FAD) in methanol-doped ice and in a deuterated solvent mixture of methanol-d-D 2 O in a large range of temperatures of 79-268 K. We found that the nonradiative process depends on the temperature, i.e., the lower
Itay Presiado, Dan Huppert
openaire   +1 more source

Inactivation of Flavine Adenine Dinucleotide by Tissue Extracts

Nature, 1948
RECENT experiments1 on the synthesis of acetylcholine by tissue extracts, especially from acetone dried brain, human placenta, and horse spleen, have shown that flavine adenine dinucleotide probably plays an essential part. It was found that spleen extracts only formed small amounts of acetylcholine under conditions giving a large synthesis with brain ...
R S, COMLINE, F R, WHATLEY
openaire   +2 more sources

A new method for preparing flavin-adenine-dinucleotide

Biochimica et Biophysica Acta, 1955
Abstract Chromatography on carboxylic resin, followed by electrophoresis on a column packed with cellulose powder, has been used to prepare pure FAD. The purity of the product has been tested spectrophotometrically, by paper chromatography and electrophoresis and by enzymic activity as coenzyme of D -amino-acid oxidase.
N, SILIPRANDI, P, BIANCHI
openaire   +2 more sources

Flavin Adenine Dinucleotide As Precursor for NADH Electrocatalyst

Analytical Chemistry, 2005
The generation of a new electrocatalytic system for NADH after oxidizing flavin adenine dinucleotide (FAD) is shown. The oxidation is performed in alkaline medium until +1.4 V (Ag/AgCl) at graphite electrodes. The catalytic activity is ascribed to the electrooxidized moiety of FAD and not to quinone surface groups.
Noemí, de-Los-Santos-Alvarez   +4 more
openaire   +2 more sources

Flavin-adenine Dinucleotide

1965
Publisher Summary This chapter discusses the determination of flavine adenine dinucleotide (FAD) that depends on the specific reactivation of the apoenzyme of D-amino acid oxidase from pig kidney by this coenzyme. Comparison of the reactivation with a standard solution of FAD is necessary because the Michaelis constant of the enzyme for F AD varies ...
openaire   +1 more source

Polarography of flavine mononucleotide and flavine adenine dinucleotide

Archives of Biochemistry and Biophysics, 1957
Abstract Flavine coenzymes FMN and FAD were studied polarographically. Both flavines show well-defined reversible polarographic waves consisting of a normal reduction wave and a “post” wave due to adsorption. The half-wave potentials of the normal reduction wave correspond to the standard oxidation-reduction potentials determined potentiometrically ...
openaire   +2 more sources

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