Behaviour and properties of catechol-O-methyltransferase from human placenta.
作者信息
Nic a' Bháird N, Tipton K F
机构信息
Department of Biochemistry, Trinity College, Dublin, Ireland.
出版信息
J Neural Transm Suppl. 1990;32:359-68. doi: 10.1007/978-3-7091-9113-2_49.
PMID:2089100
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.
摘要
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