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RECORD NUMBER: 4 OF 22

Main Title Binding of Chloroform to the Cysteine of Hemoglobin.
Author Pereira, M. A. ; Chang, L. W. ; Ferguson, J. L. ; Couri, D. ;
CORP Author Health Effects Research Lab., Cincinnati, OH. ;Ohio State Univ., Columbus.
Year Published 1984
Report Number EPA/600/J-84/131;
Stock Number PB85-123933
Additional Subjects Chloroform ; Chemical bonds ; Cysteine ; Hemoglobin ; Laboratory animals ; Rats ; Metabolism ; Gas chromatography ; Mass spectroscopy ; Chemical analysis ; Reprints ; Cysteine/N-hydroxymethyl ; Thiazolidine carboxylic acid/hydroxy
Holdings
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Status
NTIS  PB85-123933 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 13p
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. (Copyright (c) 1984 Elsevier Scientific Publishers Ireland Ltd.)