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פותח על ידי קלירמאש פתרונות בע"מ -
Role of diethyldithiocarbamate in ethylene dibromide metabolism and covalent binding
Year:
1981
Authors :
נחתומי, עדנה
;
.
Volume :
57
Co-Authors:
Nachtomi, E., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Facilitators :
From page:
247
To page:
253
(
Total pages:
7
)
Abstract:
Diethyldithiocarbamate (DDC) pretreatment of rats prevented the ethylene dibromide (EDB) depression of liver glutathione (GSH) 2 hr after toxication. The levels of cytochrome P-450 seem to by unaffected by EDB. The steady-state kinetics of the reaction of GSH with [U-14C]EDB in vitro, in the presence of glutathione-S-transferase, was determined by GSH utilization and the formation of a labeled nonvolatile product. The inhibition of the enzyme by DDC is noncompetitive producing a change in Vmax without a change in Km. DDC also inhibited the covalent binding of [14C]EDB to microsomal proteins in the microsomal system supplemented with NADPH. EDB bound to microsomal protein in the absence of NADPH. The role of DDC in the metabolism and covalent binding of EDB to macromolecules is discussed. © 1981.
Note:
Related Files :
Animal
animal experiment
covalent bond
ethylene bromide c 14
oral drug administration
Short survey / mini-review
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0041-008X(81)90286-6
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23750
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:02
Scientific Publication
Role of diethyldithiocarbamate in ethylene dibromide metabolism and covalent binding
57
Nachtomi, E., Institute of Animal Science, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Role of diethyldithiocarbamate in ethylene dibromide metabolism and covalent binding
Diethyldithiocarbamate (DDC) pretreatment of rats prevented the ethylene dibromide (EDB) depression of liver glutathione (GSH) 2 hr after toxication. The levels of cytochrome P-450 seem to by unaffected by EDB. The steady-state kinetics of the reaction of GSH with [U-14C]EDB in vitro, in the presence of glutathione-S-transferase, was determined by GSH utilization and the formation of a labeled nonvolatile product. The inhibition of the enzyme by DDC is noncompetitive producing a change in Vmax without a change in Km. DDC also inhibited the covalent binding of [14C]EDB to microsomal proteins in the microsomal system supplemented with NADPH. EDB bound to microsomal protein in the absence of NADPH. The role of DDC in the metabolism and covalent binding of EDB to macromolecules is discussed. © 1981.
Scientific Publication
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