Binding of chloroform to the cysteine of hemoglobin |
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Authors: | M A Pereira L W Chang J L Ferguson D Couri |
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Institution: | 1. U.S. Environmental Protection Agency, Health Effects Research Laboratory, 26 W. St. Clair St., Cincinnati, OH 45268 U.S.A.;2. Ohio State University, Division of Toxicology, Columbus, OH 43210 U.S.A. |
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Abstract: | 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. |
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Keywords: | Chloroform Hemoglobin Protein binding Adduct to cysteine 2-Hydroxythiazolidine-4-carboxylic acid GC gas chromatography MS mass spectrometry TLC thin-layer chromatography |
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