Behaviour and properties of catechol-O-methyltransferase from human placenta
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.
KeywordsPotassium Phosphate Buffer Ammonium Sulphate Buffer Concentration Relative Molecular Mass Potassium Acetate
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