Hooker, A.D. and James, D.C. (1998) The glycosylation heterogeneity of recombinant human IFN-gamma. Journal of Interferon and Cytokine Research, 18 (5). pp. 287-295. ISSN 1079-9907.
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The cloning of the cDNA for human interferon-gamma (IFN-gamma) has resulted in its expression in Escherichia coli, baculovirus-infected insect cells, Chinese hamster ovary (CHO) cells, and the mammary gland of transgenic mice. Large quantities of highly purified recombinant IFN-gamma have been generated, aided by the use of highly specific neutralizing monoclonal antibodies, with a view to its production as a human therapeutic protein. The primary source of structural heterogeneity for IFN-gamma during its production in mammalian expression systems is glycosylation, which can profoundly affect the three-dimensional structure of a glycoprotein and its biological function. A number of analytical approaches have been developed recently to allow a detailed analysis of the carbohydrate structures associated with IFN-gamma, the principal advances being in the areas of capillary electrophoresis and mass spectrometry, The implementation of these high-resolution analytical tools to determine the glycosylation profile of IFN-gamma makes it one of the best characterized recombinant glycoproteins, Recombinant human IFN-gamma acts as a model secretory glycoprotein, typifying the intrinsic glycosylation processing events associated with production of a potential therapeutic glycoprotein.
|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:||09 Jul 2009 09:54|
|Last Modified:||25 Jun 2012 13:39|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/17816 (The current URI for this page, for reference purposes)|
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