Control of column influence on the wide range pH gradient in ion-exchange chromatography

1992 ◽  
Vol 33 (5-6) ◽  
pp. 231-236 ◽  
Author(s):  
K. Slais ◽  
Z. Friedl
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Ph Gradient ◽  
Wide Range

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

scholarly journals Production of amylases by Aspergillus tamarii

1999 ◽  
Vol 30 (2) ◽  
pp. 157-162 ◽  
Author(s):  
Fabiana Guillen Moreira ◽  
Francieli Arrias de Lima ◽  
Sophia Renata Fazzano Pedrinho ◽  
Veridiana Lenartovicz ◽  
Cristina Giatti Marques de Souza ◽  
...  
Keyword(s):  
Carbon Source ◽  
Ion Exchange ◽  
Filamentous Fungus ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Aspergillus Tamarii ◽  
Ph Values ◽  
Wide Range ◽  
Initial Culture ◽  
Static Cultivation

A strain of Aspergillus tamarii, a filamentous fungus isolated from soil, was able to produce both <FONT FACE="Symbol">a</FONT>-amylase and glucoamylase activities in mineral media supplemented with 1% (w/v) starch or maltose as the carbon source. Static cultivation led to significantly higher yields than those obtained using shaking culture. The production of amylases was tolerant to a wide range of initial culture pH values (from 4 to 10) and temperature (from 25 to 42oC). Two amylases, one <FONT FACE="Symbol">a</FONT>-amylase and one glucoamylase, were separated by ion exchange chromatography. Both partially purified enzymes had optimal activities at pH values between 4.5 and 6.0 and were stable under acid conditions (pH 4.0-7.0). The enzymes exhibited optimal activities at temperatures between 50o and 60o C and were stable for more than ten hours at 55oC.

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