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Characterization of metastable intermediates of enzymatic peroxidation of NAD + by on‐line capillary electrophoresis/electrospray ionization mass spectrometry
Author(s) -
Zhao Zhongxi Zack,
Udseth Harold R.,
Smith Richard D.
Publication year - 1996
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/(sici)1096-9888(199602)31:2<193::aid-jms282>3.0.co;2-7
Subject(s) - chemistry , electrospray ionization , mass spectrometry , capillary electrophoresis , nad+ kinase , nicotinamide adenine dinucleotide , chromatography , reaction intermediate , electrospray , hydrogen peroxide , alcohol dehydrogenase , alcohol , enzyme , organic chemistry , catalysis
The unstable intermediate products formed from the degradation of nicotinamide adenine dinucleotide (NAD + ) catalyzed by the reaction of equine liver alcohol dehydrogenase with hydrogen peroxide were studied. Reversed anionic capillary electrophoresis (CE)/electrospray ionization mass spectrometry (ESI‐MS) was used to separate the reaction mixture and to monitor the reaction process, and to provide both molecular weight and structural information for the interaction intermediates. The mass spectra of the reaction intermediates provide support for the reaction mechanism previously proposed by Favilla et al. The present results also indicate that a different reaction intermediate may also be involved in the interaction, and contributes to the reaction. The results illustrate the utility of combined CE and ESI‐MS for the on‐line study of biochemical processes.