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Lookup NU author(s): Dr Ian West
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Coupled interrelations occurring between a phosphatase/kinase reaction sequence acting in unstirred layers and on both sides of a charged biomembrane pore structure are presented as a plausible kinetic model for the primary active transport of phosphorylated molecules. Simulations conducted at the cell level and with credible numerical values demonstrate that the enzymes positions strongly regulate the membrane permeability for the transported substrate. Depending on both the enzymes positions (more or less far from the membrane) and the membrane charges, the membrane may appear either impervious, either permeable or able to actively transport a phosphorylated substrate. Globally all happens as if, in function of the enzymes positions, a permanent pore may be regulated, changing from a more closed to a more open conformation. (C) 2002 Elsevier Science Ltd. All rights reserved.
Author(s): Maisterrena B, Fiaty K, Charcosset C, Perrin B, Couturier R, West IC
Publication type: Review
Publication status: Published
Journal: Progress in Biophysics & Molecular Biology
Year: 2002
Volume: 80
Issue: 3
Pages: 109-137
ISSN (print): 0079-6107
ISSN (electronic): 1873-1732
URL: http://dx.doi.org/10.1016/S0079-6107(02)00016-0
DOI: 10.1016/S0079-6107(02)00016-0
