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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.

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author
organization
publishing date
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
ISSN
1572-6495
DOI
10.1016/0378-4347(96)00117-X
language
English
LU publication?
yes
id
43c94bdc-e9cf-4ed4-a91f-da30bf27b284
date added to LUP
2016-04-11 13:18:36
date last changed
2016-10-05 13:46:48
@misc{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},
  keyword      = {catechol-O-methyltransferase,enzymes,reviews,protein purification},
  language     = {eng},
  month        = {07},
  number       = {1-2},
  pages        = {147--161},
  publisher    = {ARRAY(0x7e10098)},
  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},
  volume       = {684},
  year         = {1996},
}