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 |
Library |
Call Number |
Additional Info |
Location |
Last Modified |
Checkout 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.) |