Carola Tilgmann
Driftchef
Purification and partial sequence analysis of the soluble catechol-o-methyltransferase from human placenta : Comparison to the rat liver enzyme
Författare
Summary, in English
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.
Publiceringsår
1991-01-31
Språk
Engelska
Sidor
995-1002
Publikation/Tidskrift/Serie
Biochemical and Biophysical Research Communications
Volym
174
Issue
2
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 0006-291X