title: Purification of rat liver soluble catechol-O-methyltransferase by high performance liquid chromatography.
abstract: The soluble form of catechol-O-methyltransferase (EC 2.1.1.6) from rat liver was purified to homogeneity by high-performance anion-exchange chromatography and high-performance gel-filtration chromatography. The specific activity of the final pool was 270 U/mg protein. The purification was 1180-fold and recovery of the enzyme activity was 15%. During this rapid and gentle purification there were no problems with loss of activity, and the estimated half of the final purified enzyme pool was 5.5 days at +4 degrees C. The only additive used was phenylmethylsulfonylfluoride in the homogenizing buffer.
authors.affiliation: Orion Pharmaceutica, Research Center, Espoo, Finland.
authors.forename: T
authors.initials: T
authors.lastname: Korkolainen
authors.forename: E
authors.initials: E
authors.lastname: Nissinen
mesh_terms: D000818:Animals; D002394:Catechol O-Methyltransferase / Q000302:isolation & purification* / Q000378:metabolism; D002845:Chromatography / Q000379:methods; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003600:Cytosol / Q000201:enzymology; D017886:Durapatite; D006882:Hydroxyapatites; D007202:Indicators and Reagents; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D006882:Hydroxyapatites; D007202:Indicators and Reagents; D017886:Durapatite; D002394:Catechol O-Methyltransferase