piperidines has been researched along with formic-acid* in 5 studies
5 other study(ies) available for piperidines and formic-acid
Article | Year |
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Characterization of hindered amine light stabilizers employing capillary electrophoresis coupled to quadrupole time-of-flight mass spectrometry.
In the current work, a fast and reliable CE method for characterizing of six hindered amine light stabilizers (HALS), technical products commonly employed as UV-stabilizing agents for various polymeric materials, is presented. These compounds can be monomeric or oligomeric species whereby there is no or only limited information available concerning purity or actual structural composition of the respective stabilizer. Using a BGE based on formic acid with 10% acetonitrile, different constituents of several HALS could be separated by CE and identified employing QTOF/MS detection. In the case of Cyasorb 3529, ten different oligomers were discovered and possible structures were suggested based on exact mass measurements. The majority of the elucidated structures is not fully congruent with the information provided by the manufacturers. Furthermore, in the case of Chimassorb 119 and Tinuvin 770 impurities or unreacted compounds remaining from the manufacturing process could be identified. Besides performing such basic characterizations of technical grade HALS, the presented method is also shown to be suitable for a reliable identification of these stabilizers in real polymer samples. Topics: Acetonitriles; Amines; Benzophenones; Chemical Industry; Decanoic Acids; Electrophoresis, Capillary; Formates; Laboratory Chemicals; Mass Spectrometry; Piperidines; Plastics | 2014 |
Facile ring-opening of azabicyclic [3.1.0]- and [4.1.0]aminocyclopropanes to afford 3-piperidinone and 3-azepinone.
Azabicyclic [3.1.0] and [4.1.0] Kulinkovich products underwent a facile reduction/fragmentation to afford a variety of 3-piperidinones and 3-azepinones, respectively, in the presence of catalytic palladium on carbon and formic acid in an atmosphere of hydrogen. Topics: Azabicyclo Compounds; Azepines; Carbon; Catalysis; Combinatorial Chemistry Techniques; Cyclopropanes; Formates; Hydrogen; Molecular Structure; Palladium; Piperidines | 2011 |
Detection and pharmacological modulation of nicotinamide mononucleotide (NMN) in vitro and in vivo.
The emerging key role of NAD-consuming enzymes in cell biology has renewed the interest in NAD resynthesis through the rescue pathways. The first step of the nicotinamide-dependent NAD-rescue pathway is operated by nicotinamide phosphoribosyl transferase (NaPRT) forming nicotinamide mononucleotide (NMN). Because of the difficulties in measuring NMN, numerous open questions exist about the pathophysiological relevance of NaPRT and NMN itself. Here, we describe a new method of fluorimetric NMN detection upon derivatization of its alkylpyridinium group with acetophenone. By adopting this method, we analyzed the kinetics of nicotinamide-dependent NAD recycling in HeLa and U937 cells. Measurement of NMN contents in subcellular fractions revealed that the nucleotide is highly enriched in mitochondria, suggesting intramitochondrial NAD synthesis. NMN increases in cells undergoing hyperactivation of the NAD-consuming enzyme poly(ADP-ribose) polymerase (PARP)-1, or exposed to gallotannin, a putative inhibitor of NMN-adenylyl transferases. Evidence that the inhibitor of NAD resynthesis FK866 selectively inhibits NaPRT having no effect on NMNAT activity is also provided. Importantly, NMN reduces NAD and ATP depletion in cells undergoing PARP-1 hyperactivation, significantly delaying cell death. Finally, we show that a single injection of FK866 in the mouse induces long-lasting (up to 16 h) but mild (approximately 20%) reduction of NMN contents in different organs, suggesting slow rate of basal NAD consumption in vivo. Data provide new information on the biochemistry and pharmacology of NAD biosynthesis, allowing a better understanding of pyridine nucleotide metabolism. Topics: Acetophenones; Acrylamides; Animals; Cell Survival; Chromatography, High Pressure Liquid; Cytokines; Enzyme Inhibitors; Formates; HeLa Cells; Humans; Male; Mice; NAD; Niacinamide; Nicotinamide Mononucleotide; Nicotinamide Phosphoribosyltransferase; Organ Specificity; Piperidines; U937 Cells | 2009 |
The role of cytochrome P4502D6 in the metabolism of paroxetine by human liver microsomes.
Paroxetine is a selective serotonin reuptake inhibitor possessing anti-depressant activity. Demethylenation of the methylenedioxy phenyl group is the initial step in its metabolism, the liberated carbon appearing in vitro as formate. A radioassay involving [14C-methylenedioxy] paroxetine was developed and used to examine the role of cytochrome P4502D6 in paroxetine metabolism by human liver microsomes. The rate of formate production was much higher in microsomes from an extensive metaboliser of debrisoquine than from a poor metaboliser. Also, demethylenation of paroxetine was inhibited by the quinidine and quinine isomer pair in microsomes from the extensive metaboliser only. These observations strongly suggested that the process was catalysed by the enzyme cytochrome P4502D6. Metabolism could not be completely inhibited by quinidine, the residual activity representing the contribution of at least one other enzyme. The ability of microsomes from a poor metaboliser of debrisoquine to demethylenate paroxetine provided further evidence for the involvement of an enzyme distinct from P4502D6. This was confirmed by kinetic analysis of the process in microsomes from both poor and extensive metabolisers. It is concluded that, in man, the initial step of paroxetine metabolism is performed by at least two enzymes, one of which is cytochrome P4502D6. Topics: Antidepressive Agents; Carbon Radioisotopes; Cytochrome P-450 CYP2D6; Cytochrome P-450 Enzyme System; Formates; Humans; In Vitro Techniques; Microsomes, Liver; Mixed Function Oxygenases; Paroxetine; Piperidines; Serotonin Antagonists | 1992 |
Differential sequence dynamics of homopolymeric and alternating AT tracts in a small plasmid DNA.
The location of OsO4 bispyridine hyper- and hyporeactivity in a small deletion derivative of plasmid ColE1 (PTC12, 1727 bp) has been determined for approximately 70% of the molecule. Thymine bases in homopolymeric (dA)n.(dT)n tracts (n greater than or equal to 4) were always found to be resistant toward OsO4 modification. DNA supercoiling did not destabilize these tracts. The extent of OsO4 bispyridine reactivity of homopolymeric (dA)n.(dT)n tracts, where n = 3, was found to be dependent on the rate of base unpairing of the sequence immediately 5' and 3' to the tract. Repressed OsO4 reactivity of thymine bases in (dA)3.(dT)3 tracts was observed if immediately both 5' and 3' to the tract were stable DNA sequences composed of GC base pairs and/or a homopolymeric (dA)n.(dT)n tract (n greater than or equal to 4). Homopolymeric tracts of n = 3 not having adjacent sequences with repressed unpairing rates did not show reduced levels of OsO4 bispyridine reactivity. Alternating d(TA)n tracts (n greater than or equal to 2) were found to exhibit hyperreactivity with OsO4. The extent of this hyperreactivity was dependent on the length of the tract and superhelical torsional stress. The distribution and frequency of homopolymeric (dA)n.(dT)n (n greater than or equal to 4) tracts in Escherichia coli promoter sequences were examined, and the possible implications of these tracts on promoter function are discussed. Topics: Base Sequence; DNA, Bacterial; DNA, Superhelical; Electrophoresis, Agar Gel; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Formates; Molecular Sequence Data; Osmium Tetroxide; Piperidines; Plasmids; Promoter Regions, Genetic | 1991 |