Characterisation of the imidazoline site on monoamine oxidase type B

• Author / Creator

  McDonald, Glen Reid

• 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.

• Subjects / Keywords

  • MAO-B
  • Phenylethylamine
  • 2-BFI
  • Enzyme kinetics
  • I2-site
  • Benzylamine
  • Monoamine oxidase
  • Imidazoline

• Graduation date

  Fall 2014

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R3280567C

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.