scholarly journals Analytical characterization of a monoclonal antibody therapeutic reveals a three-light chain species that is efficiently removed using hydrophobic interaction chromatography

mAbs ◽  
2013 ◽  
Vol 5 (6) ◽  
pp. 925-935 ◽  
Author(s):  
Rachel B Wollacott ◽  
Paul L Casaz ◽  
Trevor J Morin ◽  
H Lily Zhu ◽  
Roger S Anderson ◽  
...  
2017 ◽  
Vol 42 (6) ◽  
Author(s):  
Şaban Keskin ◽  
Nagihan Saglam Ertunga

AbstractObjective:In this study, α-amylase from a thermophilic bacterium Geobacillus sp. TF14 was purified and immobilized on two different supports.Methods:Ion exchange and hydrophobic interaction chromatography techniques were employed for the purification.Results:The enzyme was purified as 17.11 fold and determined as a single band of 54 kDa on SDS-PAGE. Purified enzyme showed two pH optimums of pH 5.00 and pH 9.00 and the enzyme is quite stable at these pHs over a period of 48 h. Purified enzyme showed maximal activity at 75°C and stability at this temperature over a period of 72 h. It was observed that CaConclusion:It can be concluded that the purified enzyme may find application in many fields of starch based industries.


2016 ◽  
Vol 32 (2) ◽  
pp. 372-381 ◽  
Author(s):  
Alexander T. Hanke ◽  
Marieke E. Klijn ◽  
Peter D. E. M. Verhaert ◽  
Luuk A. M. van der Wielen ◽  
Marcel Ottens ◽  
...  

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