title: Behaviour and properties of catechol-O-methyltransferase from human placenta.
abstract: A procedure is reported for the purification of human placental catechol-O-methyltransferase. The preparation is apparently homogeneous and behaves as a monomer with an approximate Mr of 23,000. The sequence of the first 21 amino acid residues from the N-terminal end of the protein is reported. The activity of the enzyme is strongly influenced by the nature of the buffer in which it is assayed.
authors.affiliation: Department of Biochemistry, Trinity College, Dublin, Ireland.
authors.forename: N
authors.initials: N
authors.lastname: Nic a' Bháird
authors.forename: K F
authors.initials: KF
authors.lastname: Tipton
mesh_terms: D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D002394:Catechol O-Methyltransferase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
chemical_list: D002394:Catechol O-Methyltransferase; D000645:Ammonium Sulfate