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Characterisation of the imidazoline site on monoamine oxidase type B
- Publication Year :
- 2014
-
Abstract
- 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.
Details
- Language :
- English
- Database :
- OpenDissertations
- Publication Type :
- Dissertation/ Thesis
- Accession number :
- ddu.oai.era.library.ualberta.ca.a2acb348.491b.4e48.b691.cc48ca66cac1