Meisami_1984_J.Neurochem_42_883

Reference

Title : Is butyrylcholinesterase of the rat CNS a membrane-bound enzyme? - Meisami_1984_J.Neurochem_42_883
Author(s) : Meisami E
Ref : Journal of Neurochemistry , 42 :883 , 1984
Abstract :

The study of Arrhenius plots for acetylcholinesterase (AChE) and butyrylcholinesterase (BCHE) activity from the rat brain and spinal cord revealed that in contrast to AChE, which exhibited biphasic Arrhenius plots with a distinct break (transition temperature) at about 16-18 degrees C, BCHE showed no evidence of discontinuity and a higher activation energy in the physiological range of temperature. The results indicate lack of lipid-protein interaction in the case of BCHE of the CNS tissue. It is inferred that BCHE, in contrast to AChE, is not bound in any significant way to cellular membranes of the CNS tissue.

PubMedSearch : Meisami_1984_J.Neurochem_42_883
PubMedID: 6693906

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Citations formats

Meisami E (1984)
Is butyrylcholinesterase of the rat CNS a membrane-bound enzyme?
Journal of Neurochemistry 42 :883

Meisami E (1984)
Journal of Neurochemistry 42 :883