| Main Title |
Study of the Binding of Sulfur to Rat Liver Microsomes which Occurs Concurrently with the Metabolism of O,O-Diethyl O-p-Nitrophenyl Phosphorothioate (Parathion) to O,O-Diethyl O-p-Nitrophenyl Phosphate (Paraoxon). |
| Author |
Davis, James E. ;
Mende., Thomas J. ;
|
| CORP Author |
Health Effects Research Lab., Research Triangle Park, N.C. Population Studies Div. ;Miami Univ., Fla. Dept. of Biochemistry. |
| Year Published |
1976 |
| Report Number |
EPA/600/J-77/084; |
| Stock Number |
PB-278 583 |
| Additional Subjects |
Pesticides ;
Sulfur ;
Ribosomes ;
Liver ;
Metabolism ;
Chemical bonds ;
Chemical reactions ;
Cysteine ;
Reprints ;
Parathion ;
Paraxon ;
Metabolites ;
Sulfides
|
| Holdings |
| Library |
Call Number |
Additional Info |
Location |
Last
Modified |
Checkout
Status |
| NTIS |
PB-278 583 |
Some EPA libraries have a fiche copy filed under the call number shown. |
|
07/26/2022 |
|
| Collation |
9p |
| Abstract |
In order to investigate the nature of the sulfur that is bound to liver microsomes concurrently with the metabolism of parathion to paraoxon, an isolated rat liver microsomal preparation was labeled with (35S) parathion and the purified product was examined by chemical degradation. Characterization of the degradation products by thin-layer chromatography indicated that the sulfur is bound as a polysulfide or hydrodisulfide formed by the combination of a reactive form of sulfur, released from parathion, with cysteine residues of the microsomal protein. Preliminary investigations revealed similar binding occurs when the microsomal preparation is replaced with purified rabbit cytochrome P-450 plus NADPH-cytochrome P-450 reductase and NADPH. (Copyright (c) 1977 by The Williams & Wilkins Co.) |
