potassium-permanganate and formic-acid

potassium-permanganate has been researched along with formic-acid* in 3 studies

Other Studies

3 other study(ies) available for potassium-permanganate and formic-acid

ArticleYear
N-nitrosodimethylamine (NDMA) as a product of potassium permanganate reaction with aqueous solutions of dimethylamine (DMA).
    Water research, 2009, Volume: 43, Issue:5

    The reactivity of permanganate with dimethylamine, as possible path of NDMA formation, has been investigated. The results have shown that potassium permanganate reaction with aqueous solutions of dimethylamine (DMA) leads to the formation of N-nitrosodimethylamine (NDMA). The contact time, the molar ratio of permanganate and DMA, pH and presence of nitrite are the key factors influencing the efficiency of NDMA formation. Significant conversion rates of DMA to NDMA were observed only for the high doses of permanganate, which were many times higher than those typically used in water treatment. This reaction however is of importance for water treatment technology, since it shows the possibility of NDMA formation as a result of oxidation of DMA. It is likely that nitrosation is the main path of the reaction. An important role of MnO2 suspension, formed as a result of permanganate reduction in NDMA formation is emphasized. Significant influence of MnO2 suspension on NDMA formation should draw our attention to the potential impact of MnO2 activated filtration beds on NDMA formation.

    Topics: Ammonia; Dimethylamines; Dimethylnitrosamine; Formates; Free Radical Scavengers; Hydrogen-Ion Concentration; Nitrates; Nitrites; Oxidation-Reduction; Potassium Permanganate; Solutions; Sulfites; Suspensions

2009
Flow injection chemiluminescence determination of naftopidil based on potassium permanganate oxidation in the presence of formaldehyde or formic acid.
    Analytical and bioanalytical chemistry, 2005, Volume: 381, Issue:4

    A flow injection method is proposed for the determination of naftopidil based upon the oxidation by potassium permanganate in a sulfuric acid medium and sensitized by formaldehyde and formic acid. The optimum chemical conditions for the chemiluminescence emission were 0.25 mM potassium permanganate and 4.0 M sulfuric acid. Two manifolds were tested and instrumental parameters such as the length of the reactor, injection volume and flow rate were compared. When using the selected manifold in the presence of 0.4 M formaldehyde, naftopidil gives a second-order calibration graph over the concentration range 0.1-40.0 mg L(-1) with a detection limit calculated (as proposed by IUPAC) of 92.5 ng mL(-1) and a standard deviation of 0.12 mg mL(-1) for ten samples of 10.0 mg L(-1) naftopidil. In the presence of 1.15 M formic acid, naftopidil gives a second-order calibration graph over the concentration range 0.05-40.0 mg L(-1) with a detection limit of 14.2 ng mL(-1) and a standard deviation of 0.37 mg mL(-1) for ten samples of 10.0 mg L(-1) naftopidil. In both cases, the determination is free from interferences from common excipients such as sucrose, glucose, lactose, starch and citric acid.

    Topics: Antihypertensive Agents; Calibration; Formaldehyde; Formates; Naphthalenes; Oxidation-Reduction; Piperazines; Potassium Permanganate; Sensitivity and Specificity

2005
Strand-specific recognition of a synthetic DNA replication fork by the SV40 large tumor antigen.
    Science (New York, N.Y.), 1992, Jun-19, Volume: 256, Issue:5064

    The mechanism by which DNA helicases unwind DNA was tested; an "unwinding complex" between the SV40 large tumor antigen (T antigen) and a DNA molecule designed to resemble a replication fork was probed. In an adenosine triphosphate (ATP)-dependent reaction, T antigen quantitatively recognized this synthetic replication fork and bound the DNA primarily as a hexamer. The T antigen bound only one of the two strands at the fork, an asymmetric interaction consistent with the 3'----5' directionality of the DNA helicase activity of T antigen. Binding to chemically modified DNA substrates indicated that the DNA helicase recognized the DNA primarily through the sugar-phosphate backbone. Ethylation of six top strand phosphates at the junction of single-stranded and double-stranded DNA inhibited the DNA helicase activity of T antigen. Neither a 3' single-stranded end on the DNA substrate nor ATP hydrolysis was required for T antigen to bind the replication fork. These data suggest that T antigen can directly bind the replication fork through recognition of a fork-specific structure.

    Topics: Adenosine Triphosphate; Antigens, Polyomavirus Transforming; Diethyl Pyrocarbonate; DNA Helicases; DNA Replication; DNA, Single-Stranded; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Ethylnitrosourea; Formates; Potassium Permanganate; Sulfuric Acid Esters; Time Factors

1992