| Title : Sheep brain pseudocholinesterase: inhibition kinetics of the partially purified enzyme by some substrate analogues - Cokugras_1993_Chem.Biol.Interact_87_259 |
| Author(s) : Cokugras AN , Tezcan EF |
| Ref : Chemico-Biological Interactions , 87 :259 , 1993 |
|
Abstract :
Pseudocholinesterase (ChE) (acylcholineacylhydrolase, EC 3.1.1.8) has been partially purified (about 270-fold) from sheep brain. The procedure included ammonium sulfate fractionation (20-80%), DEAE-Trisacryl M chromatography and procainamide-Sepharose 4B affinity chromatography. The molecular weight of purified ChE was found to be 290,000 by gel filtration. Kinetic properties of the enzyme have been studied using the substrate analogues choline, succinylcholine and benzoylcholine. It was shown that the inhibition was partially competitive. |
| PubMedSearch : Cokugras_1993_Chem.Biol.Interact_87_259 |
| PubMedID: 8343984 |
| Inhibitor | Procainamide |
Cokugras AN, Tezcan EF (1993)
Sheep brain pseudocholinesterase: inhibition kinetics of the partially purified enzyme by some substrate analogues
Chemico-Biological Interactions
87 :259
Cokugras AN, Tezcan EF (1993)
Chemico-Biological Interactions
87 :259