Purification methods of mammalian catechol-O-methyltransferase
(1996) In Journal of chromatography. B, Biomedical applications 684(1-2). p.147-161- Abstract
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.
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https://lup.lub.lu.se/record/43c94bdc-e9cf-4ed4-a91f-da30bf27b284
- author
- Tilgmann, Carola LU and Ulmanen, Ismo
- publishing date
- 1996-07-20
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- catechol-O-methyltransferase, enzymes, reviews, protein purification
- in
- Journal of chromatography. B, Biomedical applications
- volume
- 684
- issue
- 1-2
- pages
- 15 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:8906471
- scopus:0030594814
- ISSN
- 1572-6495
- DOI
- 10.1016/0378-4347(96)00117-X
- language
- English
- LU publication?
- no
- id
- 43c94bdc-e9cf-4ed4-a91f-da30bf27b284
- date added to LUP
- 2016-04-11 13:18:36
- date last changed
- 2024-01-04 01:10:47
@article{43c94bdc-e9cf-4ed4-a91f-da30bf27b284, abstract = {{<p>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.</p>}}, author = {{Tilgmann, Carola and Ulmanen, Ismo}}, issn = {{1572-6495}}, keywords = {{catechol-O-methyltransferase; enzymes; reviews; protein purification}}, language = {{eng}}, month = {{07}}, number = {{1-2}}, pages = {{147--161}}, publisher = {{Elsevier}}, series = {{Journal of chromatography. B, Biomedical applications}}, title = {{Purification methods of mammalian catechol-O-methyltransferase}}, url = {{http://dx.doi.org/10.1016/0378-4347(96)00117-X}}, doi = {{10.1016/0378-4347(96)00117-X}}, volume = {{684}}, year = {{1996}}, }