Title : The kinetic properties of human placental choline acetyltransferase - Morris_1971_Biochem.J_125_857 |
Author(s) : Morris D , Maneckjee A , Hebb CO , Maneckjec A |
Ref : Biochemical Journal , 125 :857 , 1971 |
Abstract :
1. Michaelis constants for human placental choline acetyltransferase were shown to be dependent on the concentration of the second substrate present. The primary plots indicate a sequential rather than a Ping Pong mechanism and are of the same type with 300mm- and 500mm-sodium chloride. 2. Similar results have been obtained with rabbit brain choline acetyltransferase. 3. Product inhibition of the forward reaction has been studied. CoA inhibits competitively with respect to acetyl-CoA and non-competitively with respect to choline. Acetylcholine inhibits competitively with respect to choline and non-competitively with respect to acetyl-CoA. No inhibition is given by acetylcholine when the enzyme is saturated with choline. 4. It is concluded that human placental choline acetyltransferase has an ordered mechanism of the Theorell-Chance type. |
PubMedSearch : Morris_1971_Biochem.J_125_857 |
PubMedID: 5145909 |
Morris D, Maneckjee A, Hebb CO, Maneckjec A (1971)
The kinetic properties of human placental choline acetyltransferase
Biochemical Journal
125 :857
Morris D, Maneckjee A, Hebb CO, Maneckjec A (1971)
Biochemical Journal
125 :857