scholarly journals Virtual protein purification: A simple exercise to introduce ph as a parameter that effects ion exchange chromatography

2017 ◽  
Vol 46 (1) ◽  
pp. 91-97 ◽  
Author(s):  
Daniel D. Clark ◽  
Daniel J. Edwards
2008 ◽  
Vol 41 (3) ◽  
pp. 200-205 ◽  
Author(s):  
Noriko Yoshimoto ◽  
Yuko Nishijima ◽  
Parvin Akbarzadehlaleh ◽  
Sachie Fujii ◽  
Mitsuyo Abe ◽  
...  

Author(s):  
Angela Boxi ◽  
Isha Parikh ◽  
Radhika B S ◽  
Shryli K S

The present review is based on papers published between 1990 and 2020 and gives Comparative information about the most common protein purification techniques Gel-Filtration, Chromatography, Ion-Exchange Chromatography, Electrophoresis, Affinity Chromatography, and Dialysis, High-Pressure Liquid Chromatography. and their applications.


2010 ◽  
Vol 72 (11-12) ◽  
pp. 1025-1034
Author(s):  
Christopher J. Morrison ◽  
J. A. Moore ◽  
Steven M. Cramer

2009 ◽  
Vol 392 (2) ◽  
pp. 174-176 ◽  
Author(s):  
Ming-Kai Chern ◽  
Wei-Jyh Shiah ◽  
Jyun-Jie Chen ◽  
Tzung-You Tsai ◽  
Hsin-Yin Lin ◽  
...  

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.


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