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INVESTIGATION OF RECOMBINANT ANTITHROMBIN III PRODUCED BY BHK CELLS DURING FERMENTATION PROCESSES
Li, Shu-Ying
Li, Shu-Ying
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Issue Date
1991
Submitted date
2024-02-28
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Abstract
Efficient recombinant protein production processes should optimize both productivity and yield. The fermentation process should also preserve the integrity and quality of the desired protein product. AT III (antithrombin III) is one of the most important serine protease inhibitors in plasma. It is an @,-glycoprotein of M, 60,000 to 64,000 containing three or four polysaccharide chains attached by N-glycosidic linkage to asparagine residues. The biological activity of AT III can be enhanced 2-3 orders of magnitude by binding with the cofactor heparin (1). Affinity chromatography of plasma-derived AT III on immobilized heparin resulted in two fractions of AT II which differ from each other in their affinity to heparin; their difference in affinity to heparin is due to different degrees of glycosylation (2). Concerns have been raised that if BHK-derived AT III exhibit the same behavior on purification as its plasma-derived counterpart. In the fermentation of AT III producing BHK (baby hamster kidney) cells, productivity was monitored and the possible influence of serum-free cultivation conditions on protein quality in termsof both integrity (against proteolytic activity) and affinity to heparin was investigated.
Citation
Protein glycosylation, 283 - 286
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Type
Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 15
ISSN
0930-4320
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ISBN
1560811846
3527283676
3527283676
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Attribution-NonCommercial-ShareAlike 4.0 International