Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme.
Catechol-o-methyltransferase from human placenta was purified 1400-fold by hydroxyapatite adsorption, ammonium sulfate precipitation, gel filtration, high performance anion- exchange and reversed-phase chromatography. The purified enzyme has an apparent molecular weight of 26.000, an isoelectric point of 5,3 and is activated ten-fold in the presence of 20mM cysteine. The enzyme shows primary structure homology to the corresponding rat liver soluble enzyme, based on the sequenced tryptic peptides.
Tilgmann
C
C
Institute of Biotechnology, University of Helsinki, Finland.
Kalkkinen
N
N
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002394:Catechol O-Methyltransferase / Q000235:genetics / Q000302:isolation & purification*; D002850:Chromatography, Gel; D005260:Female; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin
D010446:Peptide Fragments; D002394:Catechol O-Methyltransferase; D014357:Trypsin