title: Purification of bovine hemoglobin via fast performance liquid chromatography.
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).
authors.affiliation: University of Notre Dame, Department of Chemical and Biomolecular Engineering, 182 Fitzpatrick Hall, Notre Dame, IN 46556, United States. mdimino1@nd.edu
authors.forename: Michael L
authors.initials: ML
authors.lastname: Dimino
authors.forename: Andre F
authors.initials: AF
authors.lastname: Palmer
mesh_terms: D000818:Animals; D000837:Anion Exchange Resins; D002417:Cattle; D002850:Chromatography, Gel / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000302:isolation & purification*
chemical_list: D000837:Anion Exchange Resins; D006454:Hemoglobins