||Binding of Chloroform to the Cysteine of Hemoglobin.
Pereira, M. A. ;
Chang, L. W. ;
Ferguson, J. L. ;
Couri, D. ;
||Health Effects Research Lab., Cincinnati, OH. ;Ohio State Univ., Columbus.
Chemical bonds ;
Laboratory animals ;
Gas chromatography ;
Mass spectroscopy ;
Chemical analysis ;
Thiazolidine carboxylic acid/hydroxy
||Most EPA libraries have a fiche copy filed under the call number shown. Check with individual libraries about paper copy.
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.)