Substituted hydrazones as derivatives of ketones in gas chromatography

Vandenheuvel, W.J.A.; Gardiner, W.L.; Horning, E. C.

doi:10.1016/s0021-9673(01)80380-0

Cited by 17 publications

(1 citation statement)

References 5 publications

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“…To 10 µmol of the aldehyde or ketone in 100 µl of 2 mol l −1 aqueous HCl–ethanol, 1 equiv. of the hydrazine derivative was added (10 µmol of 2,4‐dinitrophenylhydrazine23 dissolved in 1 ml 2 mol l −1 aqueous HCl–ethanol; 10 µmol of aminopiperidine24 or N , N ‐dimethylhydrazine dissolved in 100 µl of ethyl acetate; 10 µmol of dansylhydrazine25 (Fig. 1(c)) dissolved in 100 µl of methanol).…”

Section: Methodsmentioning

confidence: 99%

Derivatization of small biomolecules for optimized matrix‐assisted laser desorption/ionization mass spectrometry

et al. 2002

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Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) is a powerful tool for the measurement of low molecular mass compounds of biological interest. The limitations for this method are the volatility of many analytes, possible interference with matrix signals or bad ionization or desorption behavior of the compounds. We investigated the application of well-known and straightforward one-pot derivatization procedures to circumvent these problems. The derivatizations tested allow the measurement and the labeling of alcohols, aldehydes and ketones, carboxylic acids, alpha-ketocarboxylic acids and amines.

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Section: Methodsmentioning

confidence: 99%

Derivatization of small biomolecules for optimized matrix‐assisted laser desorption/ionization mass spectrometry

et al. 2002

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The oxidation of chiral alcohols catalyzed by catalase in organic solvents

Magner

Klibanov

1995

Biotech & Bioengineering

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The catalytic properties of bovine liver catalase have been investigated in organic solvents. In tetrahydrofuran, dioxane, and acetone (all containing 1% to 3% of water), the enzyme breaks down tert-butyl hydroperoxide several fold faster than in pure water. Furthermore, the rate of catalase-catalyzed production of tert-butanol from tert-butyl hydroperoxide increases more than 400-fold upon transition from aqueous buffer to ethanol a s the reaction medium. The mechanistic rationale for this striking effect is that in aqueous buffer the rate-limiting step of the enzymatic process involves the reduction of catalase's compound I by tert-butyl hydroperoxide. In ethanol, an additional step in the reaction scheme becomes available in which ethanol, greatly outcompeting the hydroperoxide, is oxidized by compound I regenerating the free enzyme. In solvents, such a s acetonitrile or tetrahydrofuran, which themselves are not oxidizable by compound I, catalase catalyzes the oxidation of numerous primary and secondary alcohols with tert-butyl hydroperoxide to the corresponding aldehydes or ketones. The enzymatic oxidation of s o m e chiral alcohols (2,3-butanediol, citronellol, and menthol) under these conditions occurs enantioselectively. Examination of the enantioselectivity for the oxidation of 2,3-butanediol in a series of organic solvents reveals a considerable solvent dependence. 0 1995 John Wiley & Sons, Inc.

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Signeur¹

1967

Guide to Gas Chromatography Literature

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Substituted hydrazones as derivatives of ketones in gas chromatography

Cited by 17 publications

References 5 publications

Derivatization of small biomolecules for optimized matrix‐assisted laser desorption/ionization mass spectrometry

Derivatization of small biomolecules for optimized matrix‐assisted laser desorption/ionization mass spectrometry

The oxidation of chiral alcohols catalyzed by catalase in organic solvents

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