Site-Directed Pegylation of Recombinant Interleukin-2 at its Glycosylation Site View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-04

AUTHORS

R J Goodson, N V Katre

ABSTRACT

We have modified recombinant interleukin-2 (rIL-2) to facilitate site-directed covalent attachment of monomethoxy polyethylene glycol (PEG). The site chosen for modification and subsequent covalent attachment with PEG (PEGylation) was the single glycosylation position found in the native interleukin-2 (IL-2). The mutant protein was expressed in E. coli, purified, and PEGylated with a PEG-maleimide reagent to obtain PEG-cys3-rIL-2. The PEG-cys3-rIL-2 had full bioactivity relative to the unmodified molecule and had an increase in hydrodynamic size sufficient to increase its systemic exposure by approximately 4 fold. This method has general applicability for modifying any therapeutic protein at a specific site and thereby alter its potency. In particular, it can be used to attach PEG to prokaryotically expressed recombinant proteins at their glycosylation sites. More... »

PAGES

343

References to SciGraph publications

Journal

TITLE

Bio/Technology

ISSUE

4

VOLUME

8

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt0490-343

    DOI

    http://dx.doi.org/10.1038/nbt0490-343

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1012668441

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1366535


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