Alkylation of Oxytocin by S-(2-Chloroethyl)glutathione and Characterization of Adducts by Tandem Mass Spectrometry and Edman Degradation

DOI: 10.1021/tx00045a013

Source and publish data:

Chemical Research in Toxicology p. 414 - 421 (1995)

Update date:2022-08-25

Topics:

Authors:

Erve, John C. L.

Deinzer, Max L.

Reed, Donald J.

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Article abstract of DOI:10.1021/tx00045a013

S-(2-Chloroethyl)glutathione (CEG), an alkylating agent formed by glutathione conjugation with 1,2-dichloroethane (DCE), is able to alkylate DNA and proteins. As a prelude to identification of specific protein alkylation sites, the peptide oxytocin was al

Full text of DOI:10.1021/tx00045a013

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