| Autor: |
Daryl G.S. Smith, Grant E. Frahm, Anita Kane, Barry Lorbetskie, Michel Girard, Michael J.W. Johnston, Terry D. Cyr |
| Jazyk: |
angličtina |
| Rok vydání: |
2015 |
| Předmět: |
|
| Zdroj: |
Data in Brief, Vol 4, Iss C, Pp 583-586 (2015) |
| Druh dokumentu: |
article |
| ISSN: |
2352-3409 |
| DOI: |
10.1016/j.dib.2015.07.024 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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