"Caveat Emptor"—Uricase

Gochman, Nathan; Schmitz, Joan M.

doi:10.1093/clinchem/18.5.492b

Cited by 2 publications

(2 citation statements)

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“…The principle of these methods is that hydrogen peroxide, liberated by action of cholesterol esterase and cholesterol oxidase on cholesterol esters (or free cholesterol), is combined with the peroxidase catalyzed oxidation of 4hydroxyphenylacetic acid to a fluorescent product, or with the peroxidase catalyzed oxidative coupling of 3-methyl-benzothiazoline-2-one hydrazone and 3-dimethyl-aminobenzoic acid to obtain a colored compound. [2,[13][14] The main advantages of these procedures over comparable methods are their short reaction time, high sensitivity and low cost. [14] In addition, ChOx from Streptomyces (strain A19249) exhibits a potent insecticidal activity.…”

Section: Introductionmentioning

confidence: 99%

Spectroelectrochemical Investigation of Cholesterol Oxidase from Streptomyces lividans at Different pH Values

Heinelt

Nöll

2019

ChemElectroChem

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Cholesterol oxidase from Streptomyces lividans (SlChOx) has been investigated by spectroelectrochemistry in the pH range between pH 5 and pH 9. SlChOx is a monomeric flavoenzyme with a molar mass of about 58 kDa that contains a non‐covalently bound flavin adenine dinucleotide (FAD) cofactor. Spectroelectrochemical measurements were carried out in the presence of different one and two electron redox mediators and methylene blue only, as methylene blue does not contribute significantly to the spectral changes between 350 nm and 500 nm. During the stepwise reduction and reoxidation, the presence of a stable singly reduced flavosemiquinone radical anion was observed. The pH dependent midpoint potentials (Em, pH7≈0 mV) and the redox potentials for the first and second transition Fl(quinone)/Fl(semiquinone rad anion) and Fl(semiquinone rad anion)/Fl(hydroquinone anion) were determined. A pH dependency of about −30 mV and −50 mV per pH unit was determined for the first and second reduction, respectively.

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Section: Introductionmentioning

confidence: 99%

Spectroelectrochemical Investigation of Cholesterol Oxidase from Streptomyces lividans at Different pH Values

Heinelt

Nöll

2019

ChemElectroChem

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“…Several techniques are used to measure hydrogen peroxide indirectly. Most of these employ the oxidation of different dyes using colorimetric, fluorescent, or chemoluminescent assays in the presence of a peroxidase enzyme as an indicator step [2][3][4][5][6][7][8]. All these methods have different degrees of sensitivity but in general they are subject to interferences especially from other peroxides and different reducing substances such as ascorbic acid [9,10].…”

Section: Introductionmentioning

confidence: 99%

Direct analysis of hydrogen peroxide by capillary electrophoresis

Shihabi

2006

Electrophoresis

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A method is described for analysis of hydrogen peroxide directly by CZE in borate buffer based on its absorption in UV light at 185 nm, without reaction with dyes. The absorption at 185 nm was about 3.5 times better than that at 214 nm. Hydrogen peroxide was generated enzymatically from glucose in aqueous solutions and in serum and was removed by the catalase enzyme. To improve the sensitivity of detection, samples were concentrated on the capillary based on stacking by ACN. The method is rapid (approximately 7 min) and specific.

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"Caveat Emptor"—Uricase

Cited by 2 publications

References 0 publications

Spectroelectrochemical Investigation of Cholesterol Oxidase from Streptomyces lividans at Different pH Values

Spectroelectrochemical Investigation of Cholesterol Oxidase from Streptomyces lividans at Different pH Values

Direct analysis of hydrogen peroxide by capillary electrophoresis

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