Abstract
Human serum albumin (HSA) is a versatile and important protein for the pharmaceutical industry (Fanali et al., Mol. Aspects Med. 33(3) (2012) 209–290). Due to the potential transmission of pathogens from plasma sourced albumin, numerous expression systems have been developed to produce recombinant HSA (rHSA) (Chen et al., Biochim. Biophys. Acta (BBA)—Gen. Subj. 1830(12) (2013) 5515–5525; Kobayashi, Biologicals 34(1) (2006) 55–59). Based on our previous study showing increased glycation of rHSA expressed in Asian rice (Frahm et al., J. Phys. Chem. B 116(15) (2012) 4661–4670), both supplier-to-supplier and lot-to-lot variability of rHSAs from a number of expression systems were evaluated using reversed phase liquid chromatography linked with MS and MS/MS analyses. The data are associated with the research article ‘Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa’ where further analysis of rHSA samples with additional biophysical methods can be found (Frahm et al., PLoS ONE 10(9) (2014) e109893). We determined that all rHSA samples expressed in rice showed elevated levels of arginine and lysine hexose glycation compared to rHSA expressed in yeast, suggesting that the extensive glycation of the recombinant proteins is a by-product of either the expression system or purification process and not a random occurrence.
Highlights
B 116(15) (2012) 4661–4670), both supplier-to-supplier and lot-to-lot variability of recombinant HSA (rHSA) from a number of expression systems were evaluated using reversed phase liquid chromatography linked with MS and MS/MS analyses
The data are associated with the research article ‘Determination of Supplier-to-Supplier and Lot-toLot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa’ where further analysis of rHSA samples with additional biophysical methods can be found (Frahm et al, PLoS ONE 10(9) (2014) e109893)
We determined that all rHSA samples expressed in rice showed elevated levels of arginine and lysine hexose glycation compared to rHSA expressed in yeast, suggesting that the extensive glycation of the recombinant n Correspondence to: Correspondence to: Biologics and Genetic Therapies Directorate Health Canada, AL 2201E, 251 Sir Frederick Banting Driveway, Ottawa, Ontario, K1A 0K9 Canada
Summary
Essentially FA-free pHSA (A3872 Lot090M7001V, Z99% purity), recombinant human serum albumin expressed in Saccharomyces cerevisiae (ScrHSA, Lot SLBD2407, Z99% purity, Albucult), O. sativa [OsrHSA, Lot SLBC7527V (OsrHSA-sig-C), Lot SLBG7405V (OsrHSA-sig-G), Lot SLBH9636V (OsrHSA-sig-H) and Lot SLBJ1196V (OsrHSA-sig-J) 100% purity, Cellastim] and Pichia pastoris (PprHSA, Lot 080M1580V, Z99% purity, Albagen) were sourced from Sigma-Aldrich (St. Louis, MO, USA). OsrHSA was obtained from eEnzyme LLC (Gaithersburg, MD, USA) (OsrHSA-phy) (Lot 20130110, 499% purity, Phyto-HSA), ScienCell Research Laboratories (Carlsbad, CA, USA) (OsrHSA-sci) (Lot BJABAA42, Z99% purity, Oryzogen) and amsbio LLC (Cambridge, MA, USA) (OsrHSA-ams) (Lot 20101008, 495% purity, ecoHSA). Recombumin (Lot PDP100106) was donated by Novozymes Biopharma (Cambridge, MA, USA). Amicon Ultra 0.5 ml 3000 Da molecular weight cut-off (MWCO) centrifugal filter devices were purchased from Millipore (Billerica, MA, USA). Vivacon 500 10 kDa molecular weight cut-off filters were from Sartorius Stadium Biotech North America (Bohemia, NY, USA)
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