Large scale expression of recombinant human Monoamine Oxidase A and B.
Pastoris strains expressing recombinant human Monoamine Oxidase.
Monoamine oxidase B (MAO B) is a flavoenzyme bound to the outer mitochondrial membrane and is responsible for oxidative deamination and subsequent degradation of dopamine as well as dietary amines in our body. Due to the lack of structural information on MAO B and the lack of enzymological studies on the purified enzyme, the reason for the observed differences between human and rat MAO Bs is not well understood. Comparative structural and functional studies of purified human and rat MAO B would facilitate interpretation of these observed differences. One of the major requirements in performing structural and functional studies on any protein is to have a suitable expression system to obtain large quantities of purified protein. Emory researchers have used P. pastoris as the host for the overexpression of recombinant human MAO B. A convenient approach has been developed for obtaining large amounts of purified recombinant human MAO B. The basic functional properties of the purified enzyme with benzylamine as a substrate have been determined and compared with the properties of the human enzyme.
An efficient approach to obtain purified recombinant human MAO A/B in homogeneous form with >90% functionality has been developed.
Publication: Newton-Vinson et al. Protein Expr Purif. 2000 20: 334-345.