potassium-bromide and thiocyanate

potassium-bromide has been researched along with thiocyanate* in 2 studies

Other Studies

2 other study(ies) available for potassium-bromide and thiocyanate

Article	Year
Characterization and anions inhibition studies of an α-carbonic anhydrase from the teleost fish Dicentrarchus labrax. Bioorganic & medicinal chemistry, 2011, Jan-15, Volume: 19, Issue:2 Carbonic anhydrase (CA; EC 4.2.1.1) was purified from the gill of the teleost fish Dicentrarchus labrax (European seabass). The purification procedure consisted of a single step affinity chromatography on Sepharose 4B-tyrosine-sulfanilamide. The enzyme was purified 84.9-fold with a yield of 58%, and a specific activity of 838.9 U/mg proteins. It has an optimum pH at 8.0; an optimum temperature at 10°C. The kinetic parameters of this enzyme were determined for its esterase activity, with 4-nitrophenyl acetate (NPA) as substrate. The following anions, H₂NSO₃⁻, I⁻, SCN⁻, NO₃⁻, NO₂⁻, N₃⁻, Br⁻, Cl⁻, SO₄²⁻, and F⁻ showed inhibitory effects on the enzyme. Sulfamic acid, iodide, and thiocyanate exhibited the strongest inhibitory action, in the micromolar range (K(i)s of 87-187 μM). NO₃⁻, NO₂⁻ and N₃⁻ were moderate inhibitors, whereas other anions showed only weak actions. All tested anions inhibited the enzyme in a competitive manner. Our findings indicate that these anions inhibit the fish enzyme in a similar manner to other α-CAs from mammals investigated earlier, but the susceptibility to various anions differs significantly between the fish and mammalian CAs. Topics: Animals; Anions; Bass; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Kinetics; Sulfonic Acids; Thiocyanates	2011
Determination of trace amounts of thiocyanate by a new kinetic procedure based on an induction period. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2007, Volume: 67, Issue:5 A new, simple and sensitive kinetic spectrophotometric method with no need for removing of interfering substances is proposed for the determination of thiocyanate ion in biological and water samples. The procedure is based on the inhibiting effect of thiocyanate on the sodium periodate-potassium bromide-meta cresol purple (MCP) system in acidic media. The induction period of the reaction is proportional to the SCN- concentration. The decolorization of meta cresol purple by the reaction products was used to monitor the reaction spectrophotometrically at 525 nm. Under optimum conditions, thiocyanate can be determined in the range of 0.02-0.8 microg ml(-1) with a 3sigma detection limit of 5 ng ml(-1). The relative standard deviations for 10 replicate determinations of 0.060, 0.10 and 0.50 microg ml(-1) thiocyanate are 3.7, 2.4 and 1.0%, respectively. This method has been successfully used to the determination of thiocyanate content in smokers and non-smokers saliva and spiked water sample. Topics: Bromides; Calibration; Chemistry Techniques, Analytical; Humans; Hydrochloric Acid; Kinetics; Periodic Acid; Potassium Compounds; Saliva; Spectrophotometry; Thiocyanates; Time Factors	2007

Article

Year

Characterization and anions inhibition studies of an α-carbonic anhydrase from the teleost fish Dicentrarchus labrax.

Bioorganic & medicinal chemistry, 2011, Jan-15, Volume: 19, Issue:2

Carbonic anhydrase (CA; EC 4.2.1.1) was purified from the gill of the teleost fish Dicentrarchus labrax (European seabass). The purification procedure consisted of a single step affinity chromatography on Sepharose 4B-tyrosine-sulfanilamide. The enzyme was purified 84.9-fold with a yield of 58%, and a specific activity of 838.9 U/mg proteins. It has an optimum pH at 8.0; an optimum temperature at 10°C. The kinetic parameters of this enzyme were determined for its esterase activity, with 4-nitrophenyl acetate (NPA) as substrate. The following anions, H₂NSO₃⁻, I⁻, SCN⁻, NO₃⁻, NO₂⁻, N₃⁻, Br⁻, Cl⁻, SO₄²⁻, and F⁻ showed inhibitory effects on the enzyme. Sulfamic acid, iodide, and thiocyanate exhibited the strongest inhibitory action, in the micromolar range (K(i)s of 87-187 μM). NO₃⁻, NO₂⁻ and N₃⁻ were moderate inhibitors, whereas other anions showed only weak actions. All tested anions inhibited the enzyme in a competitive manner. Our findings indicate that these anions inhibit the fish enzyme in a similar manner to other α-CAs from mammals investigated earlier, but the susceptibility to various anions differs significantly between the fish and mammalian CAs.

Topics: Animals; Anions; Bass; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Kinetics; Sulfonic Acids; Thiocyanates

2011

Determination of trace amounts of thiocyanate by a new kinetic procedure based on an induction period.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2007, Volume: 67, Issue:5

A new, simple and sensitive kinetic spectrophotometric method with no need for removing of interfering substances is proposed for the determination of thiocyanate ion in biological and water samples. The procedure is based on the inhibiting effect of thiocyanate on the sodium periodate-potassium bromide-meta cresol purple (MCP) system in acidic media. The induction period of the reaction is proportional to the SCN- concentration. The decolorization of meta cresol purple by the reaction products was used to monitor the reaction spectrophotometrically at 525 nm. Under optimum conditions, thiocyanate can be determined in the range of 0.02-0.8 microg ml(-1) with a 3sigma detection limit of 5 ng ml(-1). The relative standard deviations for 10 replicate determinations of 0.060, 0.10 and 0.50 microg ml(-1) thiocyanate are 3.7, 2.4 and 1.0%, respectively. This method has been successfully used to the determination of thiocyanate content in smokers and non-smokers saliva and spiked water sample.

Topics: Bromides; Calibration; Chemistry Techniques, Analytical; Humans; Hydrochloric Acid; Kinetics; Periodic Acid; Potassium Compounds; Saliva; Spectrophotometry; Thiocyanates; Time Factors

2007