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RECORD NUMBER: 4 OF 21

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
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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.)
Supplementary Notes Prepared in cooperation with Ohio State Univ., Columbus.
Availability Notes Pub. in Chemico-Biological Interactions 51, p115-124 1984.
NTIS Title Notes Journal article.
Title Annotations Reprint: Binding of Chloroform to the Cysteine of Hemoglobin.
PUB Date Free Form c1984
Category Codes 7D; 6A; 6E; 57B; 57U; 99F; 99A
NTIS Prices Not available NTIS
Primary Description 600/11
Document Type NT
Cataloging Source NTIS/MT
Control Number 504625266
Origin NTIS
Type CAT