Purification of IgG from Sera of Rabbit and Guinea Pig by Flow-Through Mode Ion-Exchange Chromatography using DEAE Sepharose Fast Flow Column

2011 ◽  
Vol 74 (3-4) ◽  
pp. 209-214 ◽  
Author(s):  
Ying Wang ◽  
Peiyin Zhang ◽  
Shujun Liu ◽  
Yongsheng Zhang ◽  
Tiesuo Zhao ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Guinea Pig ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Flow Through ◽  
Fast Flow

Behavior of weakly adsorbing protein impurities in flow-through ion-exchange chromatography

2021 ◽  
pp. 462788
Author(s):  
Chase E. Herman ◽  
Xuankuo Xu ◽  
Steven J. Traylor ◽  
Sanchayita Ghose ◽  
Zheng Jian Li ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Flow Through

Preparation and properties of a new dalargine analogue L-Tyr-D-Ala-Gly-L-Phe-L-Tle-L-Arg

1987 ◽  
Vol 52 (7) ◽  
pp. 1867-1871 ◽  
Author(s):  
Jan Pospíšek ◽  
Zhanna D. Bespalova ◽  
Eva Kovaříková ◽  
Michail I. Titov ◽  
Tomislav Barth ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Guinea Pig ◽  
Trifluoroacetic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Guinea Pig Ileum ◽  
Stepwise Synthesis ◽  
Biologic Activity

Stepwise synthesis in solution provided tert-butyloxycarbonyl-O-benzyl-L-tyrosyl-D-alanyl-glycyl-L-phenylalanyl-L-tert-leucyl-L-arginine which was then catalytically reduced and treated with trifluoroacetic acid. The product was purified by ion exchange chromatography and free electrophoresis. The hexapeptide containing L-tert-leucine in position 5 exhibited 63% biologic activity (guinea pig ileum) of Dalargine (L-Tyr-D-Ala-Gly-L-Phe-L-Leu-L-Arg).

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

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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