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BINDING OF CHLOROFORM TO THE CYSTEINE OF HEMOGLOBIN
Citation:
Pereira, M., L. Chang, J. Ferguson, AND D. Couri. BINDING OF CHLOROFORM TO THE CYSTEINE OF HEMOGLOBIN. U.S. Environmental Protection Agency, Washington, D.C., EPA/600/J-84/131 (NTIS PB85123933), 1984.
Description:
The products of the covalent binding of chloroform to rat hemoglobin during microsomal metabolism were isolated and identified by gas chromatography (GC) and mass spectroscopy (MS). After isolation by Proteinase K hydrolysis, amino acid analysis and cellulose thin-layer chromatography (TLC), the major product was identified by GC/MS as N-hydroxymethyl cysteine and a minor product as 2-hydroxythiazolidine-4-carboxylic acid. N-Hydroxymethyl cysteine is proposed to be formed during isolation from the 2-oxothiazolidine-4-carboxylic acid present in the intact hemoglobin. (Copyright (c) 1984 Elsevier Scientific Publishers Ireland Ltd.)