Biomedical Engineering Reference
In-Depth Information
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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