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Recombinant human interferon-gamma. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture.

Abstract:

Recombinant human interferon-gamma (Hu-IFN-gamma) produced by Chinese-hamster ovary (CHO) cells was analysed by immunoprecipitation and SDS/PAGE. Up to twelve molecular-mass variants were secreted by this cell line. Three variants were recovered after enzymic removal of all N-linked oligosaccharides or when glycosylation was inhibited by tunicamycin. The presence of three polypeptide forms rather than a single form suggested that proteolytic cleavage had occurred at two sites in both the glyc...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
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Journal:
Biochemical journal
Volume:
272
Issue:
2
Pages:
333-337
Publication date:
1990-12-01
EISSN:
1470-8728
ISSN:
0264-6021
Source identifiers:
5854
Language:
English
Keywords:
Pubs id:
pubs:5854
UUID:
uuid:fe0754d6-caa0-4611-b726-e702a00b8427
Local pid:
pubs:5854
Deposit date:
2012-12-19

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