𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Glucose-limited chemostat culture of chinese hamster ovary cells producing recombinant human interferon-γ

✍ Scribed by Paul M. Hayter; Elisabeth M. A. Curling; Anthony J. Baines; Nigel Jenkins; Ian Salmon; Phillip G. Strange; Jeremy M. Tong; Alan T. Bull


Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
870 KB
Volume
39
Category
Article
ISSN
0006-3592

No coin nor oath required. For personal study only.

✦ Synopsis


A Chinese hamster ovary (CHO) cell line expressing recornbinant human interferon-y (IFN-y) was grown under glucose limitation in a chemostat at a constant dilution rate of 0.015 h-' with glucose feed concentrations of 2.75 mM and 4 2 5 mM. The changes in cell concentration that accompanied changes in the glucose feed concentration indicated that the cells were glucose-limited. The cell yield on glucose remained constant, but there was a decline in residual glucose concentration and a reduced lactate yield from glucose in the latter stages of the culture. The consumption rates for many of the essential amino acids were increased later in the culture. The volumetric rate of interferon-y production was maintained throughout the course of this culture, indicating that IFN-y expression was stable under these conditions. However, the specific rate of IFN-y production was significantly lower at the higher glucose feed concentration. Under glucose limitation, the proportion of fully glycosylated IFN-y produced by these cells was less than that produced in the early stages of batch cultures. The proportion of fully glycosylated IFN-y increased during transient periods of glucose excess, suggesting that the culture environment influences the glycosylation of IFN-y


📜 SIMILAR VOLUMES


Site- and branch-specific sialylation of
✍ Xuejun Gu; Bryan J. Harmon; Daniel I.C. Wang 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 183 KB 👁 1 views

Since sialic acid content is known to be a critical determinant of the biological properties of glycoproteins, it is essential to characterize and monitor sialylation patterns of recombinant glycoproteins intended for therapeutic use. This study reports site-and branchspecific differences in sialyla

Metabolic effects on recombinant interfe
✍ Gregg B. Nyberg; R. Robert Balcarcel; Brian D. Follstad; Gregory Stephanopoulos; 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 199 KB 👁 1 views

Asparagine linked (N-linked) glycosylation is an important modification of recombinant proteins, because the attached oligosaccharide chains can significantly alter protein properties. Potential glycosylation sites are not always occupied with oligosaccharide, and site occupancy can change with the

Influence of Primatone RL supplementatio
✍ Xuejun Gu; Liangzhi Xie; Bryan J. Harmon; Daniel I. C. Wang 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 116 KB 👁 1 views

Although serum-free media have been widely used in mammalian cell culture for therapeutic protein production, the effects of serum-substitutes on product quality have not been extensively examined. This study observed an adverse effect of Primatone RL, an animal tissue hydrolysate commonly used as a

Improvement of interferon-γ sialylation
✍ Xuejun Gu; Daniel I. C. Wang 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 94 KB 👁 1 views

Because the presence of sialic acid can extend circulatory lifetime, a high degree of sialylation is often a desirable feature of therapeutic glycoproteins. In this study, the incomplete intracellular sialylation of interferon-␥ (IFN-␥), produced by Chinese hamster ovary cell culture, was minimized