| Literature DB >> 17581802 |
Michael L Dimino1, Andre F Palmer.
Abstract
Bovine hemoglobin (bHb) was purified from bovine red blood cells (bRBCs) via anion exchange chromatography preceded by dialysis. This is a fast and effective way to obtain bHb from bRBCs using Q Sepharose XL, a strong anion exchange resin. This resin had double the binding capacity for bHb compared to three other anion exchange resins that were studied in this work. Methemoglobin levels remained below 2% with bHb concentrations between 0.7 and 1.7 mM. The high purity of bHb was confirmed via SDS-PAGE and size exclusion chromatography (SEC).Entities:
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Year: 2007 PMID: 17581802 PMCID: PMC1994826 DOI: 10.1016/j.jchromb.2007.05.040
Source DB: PubMed Journal: J Chromatogr B Analyt Technol Biomed Life Sci ISSN: 1570-0232 Impact factor: 3.205