Selection of pH-related parameters in ion-exchange chromatography using pH-gradient operations

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 ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Gradient ◽  
Selection Of

Mixed-Bed Ion Exchange Chromatography Employing a Salt-Free pH Gradient for Improved Sensitivity and Compatibility in MudPIT

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
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Gradient ◽  
Mixed Bed Ion Exchange

pH-gradient ion-exchange chromatography: An analytical tool for design and optimization of protein separations

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 ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Analytical Tool ◽  
Ph Gradient ◽  
Protein Separations ◽  
Design And Optimization

scholarly journals The use of pH-gradient ion-exchange chromatography to separate sheep liver cytoplasmic aldehyde dehydrogenase from mitochondrial enzyme contamination, and observations on the interaction between the pure cytoplasmic enzyme and disulfiram

1981 ◽  
Vol 199 (3) ◽  
pp. 573-579 ◽  
Author(s):  
F M Dickinson ◽  
G J Hart ◽  
T M Kitson
Keyword(s):  
Ion Exchange ◽  
Aldehyde Dehydrogenase ◽  
Active Sites ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Gradient ◽  
Original Activity ◽  
Covalent Interaction ◽  
Cytoplasmic Enzyme ◽  
Sheep Liver

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.

Semiautomated pH Gradient Ion-Exchange Chromatography of Monoclonal Antibody Charge Variants

2014 ◽  
Vol 86 (19) ◽  
pp. 9794-9799 ◽  
Author(s):  
Mohammad Talebi ◽  
Robert A. Shellie ◽  
Emily F. Hilder ◽  
Nathan A. Lacher ◽  
Paul R. Haddad
Keyword(s):  
Monoclonal Antibody ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Gradient ◽  
Charge Variants
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