Role of Environmental-Conditions On the Expression Levels, Glycoform Pattern and Levels of Sialyltransferase for Hfsh Produced by Recombinant Cho Cells

Chotigeat, W, Watanapokasin, Y, Mahler, S and Gray, PP (1994). Role of Environmental-Conditions On the Expression Levels, Glycoform Pattern and Levels of Sialyltransferase for Hfsh Produced by Recombinant Cho Cells. In: Cytotechnology. Cell Culture Engineering IV Conference, San Diego Ca, (217-221). Mar 07-12, 1994. doi:10.1007/BF00762396


Author Chotigeat, W
Watanapokasin, Y
Mahler, S
Gray, PP
Title of paper Role of Environmental-Conditions On the Expression Levels, Glycoform Pattern and Levels of Sialyltransferase for Hfsh Produced by Recombinant Cho Cells
Conference name Cell Culture Engineering IV Conference
Conference location San Diego Ca
Conference dates Mar 07-12, 1994
Proceedings title Cytotechnology   Check publisher's open access policy
Journal name Cytotechnology   Check publisher's open access policy
Place of Publication DORDRECHT
Publisher SPRINGER
Publication Year 1994
Year available 1994
Sub-type Fully published paper
DOI 10.1007/BF00762396
Open Access Status DOI
ISSN 0920-9069
Volume 15
Issue 1-3
Start page 217
End page 221
Total pages 5
Language eng
Abstract/Summary A recombinant CHO cell line in which the expresison of human follicle stimulating hormone (hFSH) was under the control of the beta actin promoter was maintained in steady state perfusion cultures on a protein free medium. The level of expression of the hFSH was controlled by varying the steady state level of dissolved oxygen (10-90% of air saturation) and of sodium butyrate (0-1.5mM). Under these conditions, the specific productivity of hFSH (q(FSH)) varied from 0.7 to 4.8 ng hFSH/10(6) cells/h. As the specific productivity of hFSH increased, there was a shift in the FSH isoforms to the lower pI fractions, corresponding to increased sialic acid content. As the specific productivity of hFSH increased, shifting the isoform distribution towards the lower pI isoforms, that the sialytransferase enzymic activity also increased.
Keyword Beta Actin
Cho
Hfsh
Perfusion Cultures
Sialyltransferase
Glycosylation
Q-Index Code E1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Conference Paper
Sub-type: Fully published paper
Collection: ResearcherID Downloads - Archived
 
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