||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.)
||Prepared in cooperation with Ohio State Univ., Columbus.
||Pub. in Chemico-Biological Interactions 51, p115-124 1984.
|NTIS Title Notes
||Reprint: Binding of Chloroform to the Cysteine of Hemoglobin.
|PUB Date Free Form
||7D; 6A; 6E; 57B; 57U; 99F; 99A
||Not available NTIS