Carola Tilgmann
Driftchef
Purification methods of mammalian catechol-O-methyltransferase
Författare
Summary, in English
The protein purification strategies used for obtaining homogeneous rat and human soluble catechol-O-methyltransferase (S-COMT) polypeptides are reviewed. Expression and purification of recombinant rat and human S-COMT in Escherichia coli and for human S-COMT in baculovirus-infected insect cells made it possible to elucidate the S-COMT polypeptides in more detail. The application of these purification methods has allowed the crystallization of the rat S-COMT protein and the analysis of the kinetic properties of the enzyme in great detail. The availability of the pure S-COMT protein together with the structural data has also greatly enhanced the development of more potent COMT inhibitors.
Publiceringsår
1996-07-20
Språk
Engelska
Sidor
147-161
Publikation/Tidskrift/Serie
Journal of chromatography. B, Biomedical applications
Volym
684
Issue
1-2
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Biochemistry and Molecular Biology
- Cell Biology
Nyckelord
- catechol-O-methyltransferase
- enzymes
- reviews
- protein purification
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1572-6495