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Glycosylation of CD4 and Thy-1.

Abstract:

The site-specific glycosylation of soluble recombinant variants of human and rat CD4 (sCD4) expressed in Chinese hamster ovary (CHO) cells has been characterized. The presence of identical oligosaccharides at the conserved glycosylation site in domain 3 of rat and human sCD4 and the greater abundance of oligomannose and hybrid type glycans at the non-conserved glycosylation site of rat sCD4 clearly indicate that the protein structure influences oligosaccharide processing. Comparisons of rat s...

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Publication status:
Published

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Publisher copy:
10.1098/rstb.1993.0133

Authors


Ashford, DA More by this author
Parekh, RB More by this author
Rademacher, TW More by this author
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Journal:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume:
342
Issue:
1299
Pages:
43-50
Publication date:
1993-10-05
DOI:
EISSN:
1471-2970
ISSN:
0962-8436
URN:
uuid:10b0d6c5-e0f5-4786-9346-be06f9abf25f
Source identifiers:
22707
Local pid:
pubs:22707

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