Biomedical Engineering Reference
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Table 3a. Nature of glycosylation in different proteins expressed in the cell line CHO
Protein expressed
Nature of glycosylation
Recombinant protein
Native protein
References
CHO
1. IFN
g
Biantennary complex type
(Asn 25 and Asn 97 )
Two glycosylation sites
[213]
2. tPA
Oligomannose type chain in one
Complex and oligomannose.
[208]
of the three N -glycosylation sites.
Three Asn sites, two classes of
Other two sites (Asn 184 and Asn 448 )
varients: type I and type II with
[212, 214]
are complex type
either Asn 117 and Asn 448 or Asn 117 ,
Asn 184 and Asn 448 respectively.Asn 117
is oligomannose type, other two are
charged complex type
3. EPO
Tetraantennary complex type at
One O -linked and three
[212, 215]
three Asn sites and one O -linked glycans.
N -linked glycans. N -linked
More O -linked glycans and less sialic
glycans are extensively
acid than native form manifest con-
branched and complex
formational differences and hence in
type structure having tetra-
the potency
antennary glycans
Table 3b. Nature of glycosylation in IFN
g
expressed in different cell lines
Protein
Cell line
Nature of glycosylation
Remarks
References
espressed
IFN
g
1. CHO
Complex biantennary
The glycans of native IFN
g
is
[191, 195, 215]
type (Asn 25 and Asn 97 )
exclusively complex biantennary
2. Sf9
Mainly trimannosyl
type. Specific activity is comparable
core structure
with the recombinant proteins,
3. Mammary gland
Intermediate glycan profile
however such heterogeneity in gly-
of transgenic mice
(complex structure at Asn 25
cans could affect the circulatory half-
and oligomannose structure at Asn 97 )
life due to varying degree of susceptibility
to clearance by Man receptors
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