Method Development Strategies for Ion Exchange Chromatography Using pH Gradient Separation for mAbs, Antibody Drug Conjugates (ADCs) and Other Complex Bio-Pharmaceuticals

2019 ◽  
pp. 415-469
Author(s):  
Norman L. Fischer ◽  
Scott Allen
mAbs ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 1113-1121
Author(s):  
Zhaorui Zhang ◽  
Shiyue Zhou ◽  
Linjie Han ◽  
Qunying Zhang ◽  
Wayne A. Pritts

2008 ◽  
Vol 1194 (1) ◽  
pp. 22-29 ◽  
Author(s):  
Tangir Ahamed ◽  
Sreekanth Chilamkurthi ◽  
Beckley K. Nfor ◽  
Peter D.E.M. Verhaert ◽  
Gijs W.K. van Dedem ◽  
...  

2013 ◽  
Vol 85 (14) ◽  
pp. 6608-6616 ◽  
Author(s):  
Geert P. M. Mommen ◽  
Hugo D. Meiring ◽  
Albert J. R. Heck ◽  
Ad P. J. M. de Jong

2007 ◽  
Vol 1164 (1-2) ◽  
pp. 181-188 ◽  
Author(s):  
Tangir Ahamed ◽  
Beckley K. Nfor ◽  
Peter D.E.M. Verhaert ◽  
Gijs W.K. van Dedem ◽  
Luuk A.M. van der Wielen ◽  
...  

1981 ◽  
Vol 199 (3) ◽  
pp. 573-579 ◽  
Author(s):  
F M Dickinson ◽  
G J Hart ◽  
T M Kitson

1. Sheep liver cytoplasmic aldehyde dehydrogenase can be purified from contamination with the mitochondrial form of the enzyme by pH-gradient ion-exchange chromatography. The method is simple, reproducible and efficient. 2. The purified cytoplasmic enzyme retains about 2% of its original activity in the presence of a large excess of disulfiram. This suggests that the disulfiram-reactive thiol groups are not essential for covalent interaction with the aldehyde substrate during catalysis, as has sometimes been suggested. 3. Between 1.5 and 2.0 molecules of disulfiram per tetrameric enzyme molecule account for the observed loss of activity, suggesting that the enzyme may have only two functional active sites. 4. Experiments show that disulfiram-modified enzyme retains the ability to bind NAD+ and NADH.


2014 ◽  
Vol 86 (19) ◽  
pp. 9794-9799 ◽  
Author(s):  
Mohammad Talebi ◽  
Robert A. Shellie ◽  
Emily F. Hilder ◽  
Nathan A. Lacher ◽  
Paul R. Haddad

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