James, David C. (1996) Analysis of recombinant glycoproteins by mass spectrometry. Cytotechnology, 22 (1-3). pp. 17-24. ISSN 0920-9069. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
The advent of new technologies for analysis of biopolymers by mass spectrometry has revolutionised strategies for recombinant protein characterization. The principal recent developments have been matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry. Using these tools, accurate molecular mass determinations can now be obtained routinely - often using minute (picomole - femtomole) quantities of protein or protein fragments. These techniques have proved indispensible for detailed characterization of the post-translational modifications of recombinant proteins produced by eukaryotic systems. Glycosylation is arguably the most important and complex of these modifications and has prompted widespread use of these new techniques. In this mini-review article I describe recent advances in the use of mass spectrometry for analysis of recombinant glycoproteins.
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||R.F. Xu|
|Date Deposited:||04 Jun 2009 16:11|
|Last Modified:||23 Apr 2014 10:58|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/19259 (The current URI for this page, for reference purposes)|