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Permanent link (DOI): https://doi.org/10.7939/R3280567C

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Characterisation of the imidazoline site on monoamine oxidase type B Open Access

Descriptions

Other title
Subject/Keyword
MAO-B
enzyme kinetics
phenylethylamine
imidazoline
benzylamine
I2-site
monoamine oxidase
2-BFI
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
McDonald, Glen Reid
Supervisor and department
Hudson, Alan (Pharmacology)
Holt, Andrew (Pharmacology)
Examining committee member and department
Hudson, Alan (Pharmacology)
Baker, Glen (Psychiatry)
Holt, Andrew (Pharmacology)
Lemieux, Joanne (Biochemistry)
Department
Department of Pharmacology
Specialization

Date accepted
2014-09-24T11:46:58Z
Graduation date
2014-11
Degree
Master of Science
Degree level
Master's
Abstract
Monoamine oxidase enzymes are largely involved in the catabolism of biogenic amines. Two forms of the enzyme are socumented to exist, monoamine oxidase type A and B. The B form (MAO-B) of the enzyme has been noted to possess a high affinity site for some imidazoline ligands. This site (the I2 site) appears to exist only on a small fraction of MAO-B enzymes but the function of the site is not known. The ligands that bind to this site with high affinity appear to inhibit catalytic activity at concentrations some 1000-fold higher than those required to bind to the I2 site. The goal of the present work was to characterise the I2 site on MAO-B through radio-ligand binding and kinetic assays. In doing so, phenylethylamine was found to create a high-affinty site for 2-BFI on MAO-B. The rate of site-formation is influenced by the presence of 2-BFI. This work represents a new understanding of MAO-B kinetics and opens the door for future research into the potential importance of the I2 site on MAO-B.
Language
English
DOI
doi:10.7939/R3280567C
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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