Preparation of Uniform Size Beads with Enhanced Hydrophilicity of Pore Surface, Based on Macrophorous Poly(glycidyl methacrylate-co-ethylene dimethacrylate)

1993 ◽  
Vol 58 (11) ◽  
pp. 2605-2611 ◽  
Author(s):  
Vladimír Šmigol ◽  
František Švec
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Size Exclusion ◽  
Uniform Size ◽  
Mobile Phases ◽  
Before And After ◽  
Ethylene Dimethacrylate ◽  
Size Exclusion Hplc ◽  
Albumin Adsorption

Relative hydrophilicity of poly(glyceryl methacrylate-co-ethylene dimethacrylate) beads before and after modification with epichlorohydrin followed by hydrolysis has been studied. The hydrophilicity was determined from the retention of human serum albumin in a column packed with the polymers using various mobile phases. Hydrophilization dramatically decreases the extent of human serum albumin adsorption and provides beads suitable for size-exclusion HPLC of hydrophobic proteins.

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.

Human serum albumin binding to silica nanoparticles – effect of protein fatty acid ligand

2014 ◽  
Vol 16 (21) ◽  
pp. 10157-10168 ◽  
Author(s):  
Joo Chuan Ang ◽  
Mark J. Henderson ◽  
Richard A. Campbell ◽  
Jhih-Min Lin ◽  
Peter N. Yaron ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Time Dependence ◽  
Human Serum ◽  
Silica Nanoparticles ◽  
Albumin Binding ◽  
Acid Ligand ◽  
Human Serum Albumin Binding ◽  
Albumin Adsorption

Fat containing and defatted human serum albumin adsorption to silica nanoparticles have different structures and time dependence to form.

Neutron and X-ray Reflectivity Studies of Human Serum Albumin Adsorption onto Functionalized Surfaces of Self-Assembled Monolayers

1997 ◽  
Vol 13 (5) ◽  
pp. 635-639 ◽  
Author(s):  
S. Petrash ◽  
A. Liebmann-Vinson ◽  
M.D. Foster ◽  
L.M. Lander ◽  
W.J. Brittain ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Self Assembled Monolayers ◽  
X Ray ◽  
Functionalized Surfaces ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Albumin Adsorption

Human Serum Albumin Adsorption Study on 62-MHz Miniaturized Quartz Gravimetric Sensors

2008 ◽  
Vol 80 (15) ◽  
pp. 5930-5936 ◽  
Author(s):  
Ping Kao ◽  
Ashish Patwardhan ◽  
David Allara ◽  
Srinivas Tadigadapa
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Adsorption Study ◽  
Gravimetric Sensors ◽  
Albumin Adsorption

Chromatographic kinetic measurements of human serum albumin adsorption on monoclonal antibodies

1995 ◽  
Vol 8 (1-2) ◽  
pp. 85-89 ◽  
Author(s):  
James Renard ◽  
Claire Vidal-Madjar ◽  
Bernard Sebille ◽  
Claude Lapresle
Keyword(s):  
Monoclonal Antibodies ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Kinetic Measurements ◽  
Albumin Adsorption
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