Modulation of CCTa by membrane biophysics
Modulation of CCTa by membrane biophysics
CCTα (CTP: phosphocholine cytidyltransferase) catalyses the rate limiting step in the synthesis of phophatidylcholine through the Kennedy pathway. CCTα, essentially inactive in solution, becomes active in the presence of lipid membranes, into which it partitions. Surface negative charge and torque tension were found to be membrane properties that modulate the enzyme activity.
Lipid monolayers and large unilamellar vesicles (LUVs) were examined as possible candidates to be used as model system of biological membranes. Using LUVs as model systems, the effect of surface charge, of torque tension and of lipid concentration on the CCTα activity were investigated.
A set of equations was derived attempting to distinguish between the partitioning of the enzyme onto vesicles and its activation. The preliminary results indicate that the torque tension affects mostly the enzyme partitioning whilst the surface charge effects mostly the enzyme activity.
University of Southampton
Fagone, Paolo
bdc0cf16-ad66-43a7-8208-13819336c44d
2003
Fagone, Paolo
bdc0cf16-ad66-43a7-8208-13819336c44d
Fagone, Paolo
(2003)
Modulation of CCTa by membrane biophysics.
University of Southampton, Doctoral Thesis.
Record type:
Thesis
(Doctoral)
Abstract
CCTα (CTP: phosphocholine cytidyltransferase) catalyses the rate limiting step in the synthesis of phophatidylcholine through the Kennedy pathway. CCTα, essentially inactive in solution, becomes active in the presence of lipid membranes, into which it partitions. Surface negative charge and torque tension were found to be membrane properties that modulate the enzyme activity.
Lipid monolayers and large unilamellar vesicles (LUVs) were examined as possible candidates to be used as model system of biological membranes. Using LUVs as model systems, the effect of surface charge, of torque tension and of lipid concentration on the CCTα activity were investigated.
A set of equations was derived attempting to distinguish between the partitioning of the enzyme onto vesicles and its activation. The preliminary results indicate that the torque tension affects mostly the enzyme partitioning whilst the surface charge effects mostly the enzyme activity.
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Published date: 2003
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Local EPrints ID: 465203
URI: http://eprints.soton.ac.uk/id/eprint/465203
PURE UUID: fc487b3e-7b55-47db-8cfc-a272620faf87
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Date deposited: 05 Jul 2022 00:29
Last modified: 16 Mar 2024 20:01
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Author:
Paolo Fagone
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