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- W2007674619 abstract "Abstract Bovine hemoglobin (HbBv) was isolated from whole blood and additionally purified by anion exchange chromatography. To obtain derivatives potentially suitable as oxygen carriers, oxidized trehalose was used as cross‐linking reagent. Intra‐ and intermolecular bonds were formed by reaction between reactive aldehyde groups of oxidized trehalose and primary amine groups on the protein surface. After reduction of the Schiff bases formed, the HbBv derivatives were characterized by high performance liquid chromatography (HPLC), electrophoresis and by ultraviolet spectroscopy to evaluate methemoglobin contents." @default.
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- W2007674619 date "2006-12-01" @default.
- W2007674619 modified "2023-09-25" @default.
- W2007674619 title "Oligomerization of Bovine Hemoglobin and Characterization of the Potential Blood Substitutes" @default.
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- W2007674619 doi "https://doi.org/10.1002/masy.200651371" @default.
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