title: [Purification of monoamine oxidase B from porcine liver].
abstract: Monoamine oxidase B (MAOB) was purified from porcine liver by solubilization with lysis buffer containing 1% Triton X-100, precipitation with 20%-50% ammonium sulfate, isolation with hydrophobic chromatography and anion exchange chromatography. The purification fold was 18.2. The specific activity was 135 U/mg. The purified enzyme appeared homogeneous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and it had a relative molecular mass of about 60,000. The identification of the enzyme was confirmed by high performance liquid chromatography-electrospray ionization tandem mass spectrometry (HPLC-ESI-MS/MS). As MAOB is a membrane enzyme, a key step to the successful purification was the use of Phenyl-Sepharose CL-4B with phenyl density of 75.7 micromol/mL. The results showed that this approach could effectively isolate MAOB from porcine liver to yield an enzyme with high purity and specific activity.
authors.affiliation: Department of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, China.
authors.forename: Jiayi
authors.initials: J
authors.lastname: Sun
authors.forename: Jun
authors.initials: J
authors.lastname: Ren
authors.forename: Li
authors.initials: L
authors.lastname: Xu
authors.forename: Lingyun
authors.initials: L
authors.lastname: Jia
mesh_terms: D000818:Animals; D002845:Chromatography / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D008099:Liver / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000302:isolation & purification*; D013552:Swine
chemical_list: D008995:Monoamine Oxidase