RECOMBINANT INTERFERON-γ SECRETED BY CHINESE HAMSTER OVARY-320 CELLS CULTIVATED IN SUSPENSION IN PROTEIN-FREE MEDIA IS PROTECTED AGAINST EXTRACELLULAR PROTEOLYSIS BY THE EXPRESSION OF NATURAL PROTEASE INHIBITORS AND BY THE ADDITION OF PLANT PROTEIN HYDROLYSATES TO THE CULTURE MEDIUM

2005 ◽  
Vol 41 (3) ◽  
pp. 83 ◽  
Author(s):  
J. MOLS ◽  
C. PEETERS-JORIS ◽  
R. WATTIEZ ◽  
S. N. AGATHOS ◽  
Y.-J. SCHNEIDER
2000 ◽  
Vol 44 (5) ◽  
pp. 770-783
Author(s):  
Gregg B. Nyberg ◽  
R. Robert Balcarcel ◽  
Brian D. Follstad ◽  
Gregory Stephanopoulos ◽  
Daniel I. C. Wang

1995 ◽  
Vol 13 (4) ◽  
pp. 389-392 ◽  
Author(s):  
Michael Zang ◽  
Helmut Trautmann ◽  
Christine Gandor ◽  
Ferruccio Messi ◽  
Fred Asselbergs ◽  
...  

1995 ◽  
Vol 307 (3) ◽  
pp. 791-797 ◽  
Author(s):  
D C A Neville ◽  
R A Field ◽  
M A J Ferguson

Several hydrophobic glycosides of N-acetylglucosamine (GlcNAc) served as primers for polylactosamine synthesis when added to Chinese hamster ovary (CHO) cells. The modified glycosides, containing one to six lactosamine repeats in linear array, were sialylated and secreted into the culture medium. The relative efficiencies of the glycosides to serve as primers were dependent on the nature of the aglycone and on the anomeric configuration of the GlcNAc residue. The same compounds were tested for their effects on glycolipid synthesis in CHO cells. All of the beta-glycosides significantly inhibited the synthesis of the lactoseries glycolipid GM3 whereas the alpha-glycoside was inactive. The compound GlcNAc alpha 1-O-benzyl- was the most efficient primer of polylactosamine synthesis and had no effect on glycolipid synthesis. This compound may have potential for the assay of the polylactosamine synthetic capacity of living cells.


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