Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme.
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Tilgmann C, Kalkkinen N
Purification and partial sequence analysis of the soluble catechol-O-methyltransferase from human placenta: comparison to the rat liver enzyme.
Biochem Biophys Res Commun. 1991 Jan 31;174(2):995-1002.
- PubMed ID
- 1993083 [ View in PubMed]
- Abstract
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.