title: Purification and partial characterization of rat liver soluble catechol-O-methyltransferase.
abstract: The rat liver soluble catechol-O-methyltransferase (EC 2.1.1.6.) has been purified utilizing a combination of conventional chromatography and HPLC. The purified enzyme has a molecular mass of 25 kDa, a pI of 5.1, and exists in two forms which differ in the nature of their intramolecular disulfide bonds. This difference causes these two protein forms to behave differently in reversed phase chromatography.
authors.affiliation: Orion Corporation, Genetic Engineering Laboratory, Helsinki, Finland.
authors.forename: C
authors.initials: C
authors.lastname: Tilgmann
authors.forename: N
authors.initials: N
authors.lastname: Kalkkinen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002394:Catechol O-Methyltransferase / Q000302:isolation & purification* / Q000378:metabolism; D002458:Cell Fractionation / Q000379:methods; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D051381:Rats; D014357:Trypsin
chemical_list: D002394:Catechol O-Methyltransferase; D014357:Trypsin