Serial Coupling of Ion-Exchange and Size-Exclusion Chromatography to Determine Aggregation Levels in mAbs in The Presence of a Proteinaceous Excipient, Recombinant Human Serum Albumin

2015 ◽  
Vol 104 (2) ◽  
pp. 548-556 ◽  
Author(s):  
Paul Luigi Gargani Weisbjerg ◽  
Mikael Bjerg Caspersen ◽  
Ken Cook ◽  
Marco Van De Weert
Keyword(s):  
Human Serum Albumin ◽  
Ion Exchange ◽  
Serum Albumin ◽  
Human Serum ◽  
Size Exclusion Chromatography ◽  
Size Exclusion ◽  
Recombinant Human Serum Albumin ◽  
Exclusion Chromatography

scholarly journals Aggregate Removal Nanofiltration of Human Serum Albumin Solution Using Nanocellulose-Based Filter Paper

Biomedicines ◽  
2020 ◽  
Vol 8 (7) ◽  
pp. 209 ◽  
Author(s):  
Lulu Wu ◽  
Athanasios Mantas ◽  
Simon Gustafsson ◽  
Levon Manukyan ◽  
Albert Mihranyan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Filter Paper ◽  
High Performance ◽  
Size Exclusion ◽  
Transmembrane Pressure ◽  
Protein Loss ◽  
Virus Removal ◽  
Model Virus

This study is dedicated to the rapid removal of protein aggregates and viruses from plasma-derived human serum albumin (HSA) product to reduce the risk of viral contamination and increase biosafety. A two-step filtration approach was implemented to first remove HSA aggregates and then achieve high model virus clearance using a nanocellulose-based filter paper of different thicknesses, i.e., 11 μm (prefilter) and 22 μm (virus filter) at pH 7.4 and room temperature. The pore size distribution of these filters was characterized by nitrogen gas sorption analysis. Dynamic light scattering (DLS) and size-exclusion high performance liquid chromatography (SE-HPLC) were performed to analyze the presence of HSA aggregates in process intermediates. The virus filter showed high clearance of a small-size model virus, i.e., log10 reduction value (LRV) > 5, when operated at 3 and 5 bar, but a distinct decrease in LRV was detected at 1 bar, i.e., LRV 2.65–3.75. The throughput of HSA was also dependent on applied transmembrane pressure as was seen by Vmax values of 110 ± 2.5 L m−2 and 63.6 ± 5.8 L m−2 at 3 bar and 5 bar, respectively. Protein loss was low, i.e., recovery > 90%. A distribution of pore sizes between 40 nm and 60 nm, which was present in the prefilter and absent in the virus filter, played a crucial part in removing the HSA aggregates and minimizing the risk of virus filter fouling. The presented results enable the application of virus removal nanofiltration of HSA in bioprocessing as an alternative to virus inactivation methods based, e.g., on heat treatment.

scholarly journals Data set for mass spectrometric analysis of recombinant human serum albumin from various expression systems

Data in Brief ◽  
2015 ◽  
Vol 4 ◽  
pp. 583-586
Author(s):  
Daryl G.S. Smith ◽  
Grant E. Frahm ◽  
Anita Kane ◽  
Barry Lorbetskie ◽  
Michel Girard ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Expression Systems ◽  
Data Set ◽  
Recombinant Human Serum Albumin

Identification of competitive inhibitors for bovine serum albumin from dynamic combinatorial libraries containing a bienzyme system

RSC Advances ◽  
2015 ◽  
Vol 5 (30) ◽  
pp. 23224-23228 ◽  
Author(s):  
Wei He ◽  
Zheng Fang ◽  
Zhao Yang ◽  
Dong Ji ◽  
Ketao Chen ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Size Exclusion Chromatography ◽  
Bovine Serum ◽  
Combinatorial Libraries ◽  
Size Exclusion ◽  
System P ◽  
Competitive Inhibitors ◽  
Exclusion Chromatography

Three dynamic combinatorial libraries (DCLs) have been generated by using esterification, combined with a protocol based on size-exclusion chromatography (SEC) and HRMS.

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