MASS-SPECTROMETRY IN THE ANALYSIS OF GLUTATHIONE CONJUGATES
MASS-SPECTROMETRY IN THE ANALYSIS OF GLUTATHIONE CONJUGATES
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DOI：
10.1002/bms.1200220602
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发表时间：
1993-06-01
期刊：
影响因子：
--
通讯作者：
DAVIS, MR
中科院分区：
文献类型：
--
作者：
BAILLIE, TA;DAVIS, MR
Glutathione (yL-glutamyl-L-cysteinylglycine, GSH; Fig. 1) is a ubiquitous tripeptide in mammalian systems, where its intracellular concentration can be as high as 10 mM.'By virtue of the nucleophilicity of its cysteinyl thiol group, GSH functions as an obligatory cofactor in many biochemical reactions and is of importance in the biosynthesis of a wide range of endogenous compounds, including prostaglandins, leukotrienes and catechol estrogens. It is also involved in the metabolism of products of heme degradation and lipid peroxidation, and contributes to the maintenance of cellular redox potential through its actions as an antioxidant and modulator of protein thiol-disulfide equilibria. In addition to the above functions in intermediary biochemistry, GSH plays an important role in the detoxification of electrophilic foreign compounds and chemically reactive intermediates which may arise during the biotransformation of xenobiotics. 2 In the latter context, GSH and S-linked conjugates thereof have become the focus of considerable interest in the fields of drug metabolism and biochemical toxi~ ology,~ where structural elucidation of GSH adducts can assume importance for a number of reasons. Firstly, since GSH conjugates may result from the reaction of the-SH moiety of GSH with potentially toxic electrophilic metabolites, the structures of the resulting adducts provide information on the identities of the (often transient) intermediates from which they were derived. Secondly, conjugation with GSH can result in the pharmacological inactivation of several chemotherapeutic alkylating agents (eg nitrogen mustards), a process which is thought to be responsible for the devel-
