Purification methods of mammalian catechol-O-methyltransferase
Tilgmann, Carola LU
and Ulmanen, Ismo
(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.
Please use this url to cite or link to this publication:
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
-
- scopus:0030594814
- pmid:8906471
- 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}},
}