Efficiency assessment of ion-exchange chromatography as the final stage of anti-VEGF antibody purification

2021 ◽  
pp. 6-9
Author(s):  
Denis Alekseevich Mazalyov ◽  
Aleksey Vladimirovich Tsivov ◽  
Viktor Andreevich Kuvshinov ◽  
Mariya Nikolaevna Zavorueva ◽  
Aleksandr Alekseevich Smirnov ◽  
...  

The article presents the results of chromatographic purification of the anti-VEGF antibody using the ion-exchange sorbent CaptoТМ S and considers the prospects for medical application of the antibody as a therapeutic agent for cancer treatment.

2001 ◽  
Vol 907 (1-2) ◽  
pp. 145-154 ◽  
Author(s):  
Heather L Knudsen ◽  
Robert L Fahrner ◽  
Yuan Xu ◽  
Lenore A Norling ◽  
Gregory S Blank

1988 ◽  
Vol 32 (3) ◽  
pp. 326-333 ◽  
Author(s):  
A. Jungbauer ◽  
F. Unterluggauer ◽  
K. Uhl ◽  
A. Buchacher ◽  
F. Steindl ◽  
...  

2020 ◽  
Vol 51 (4) ◽  
pp. 1195-1203
Author(s):  
Noori & Aziz

This study was aimed to purify, characteristic, and fibrinolytic activity of staphylokinase (SAK), is an enzyme activates plasminogen to form plasmin, which digest fibrin clots that cause thrombosis clot. Staphylokinase was purified from local isolate Staphylococcus aureus GH38 by ammonium sulfate precipitation at 70% saturation followed by ion exchange chromatography (CM-Cellulose) with a purification fold 2.73, and 1.53, and recovery 72.1, and 33.11% in wash and elution steps respectively. The partially purified enzyme was high activity at 40°C with pH 7 and the enzyme retained 100% of its activity at 35°C with pH 7. The activity of an enzyme increased by its treatment with calcium and sodium chloride, while the activity affected when incubated with mercury, silver, and iron chloride. The enzyme have high effective against thrombus (blood clot), which encourage the use of enzyme in the treatment as therapeutic agent to remove clots formed in the human body.


2018 ◽  
Vol 33 (4) ◽  
pp. 613-628 ◽  
Author(s):  
K. K. Larsen ◽  
D. Wielandt ◽  
M. Bizzarro

We present a refined multi-element (Mg, Ca, Ti, V, Cr, Fe, Ni, Zr, Mo, Ru, Hf and W) ion chromatographic purification protocol applied to high-precision isotope analysis of Mg and Ti using MC-ICP-MS.


2015 ◽  
Vol 16 (2) ◽  
pp. 107-113 ◽  
Author(s):  
Tobias Hahn ◽  
Thiemo Huuk ◽  
Anna Osberghaus ◽  
Katharina Doninger ◽  
Susanne Nath ◽  
...  

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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