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Evaluation of Anion-exchange Liquid Chromatography for Purification of Hemoglobin from Peptides and Other Proteins. by Jan Simoni; Grazyna Simoni; Mario Feola; Peter C Canizaro is a Chemistry article available to read on EtoBox.

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## Solutions of hemoglobin (Hb) are under development for use as "red blood cell substitutes". In order to reduce the presence of immunogenic and vasoactive factors in these solutions, the elimination of non-Hb proteins and peptides is necessary. The ability of anion-exchange liquid chromatography (LC) to purify Hb, using the Waters HPLC 600E system and five different columns (HP-PEI, MA7P, DEAE-SPW, MA7Q and Mono-Q HR) was evaluated. Bovine Hb, prepared by hyposmotic dialysis-ultrafiltration of isolated red blood cells, was subjected to chromatography by each column. The major fraction (HbAo) was analyzed by re-separation through the same column and by isoelectric focusing (IEF) with silver staining. The second chromatogram revealed HbAo to contain 2-4 non-Hb contaminants, some of which adherent to and some separate from hemoglobin. IEF revealed the full spectrum of Hb contamination, with 3-5 protein bands plus lo-15 peptide bands in association with HbAo. The results suggest that anion-exchange cannot completely purify hemoglobin and IEF with silver staining is more sensitive than LC.

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Author

Jan Simoni; Grazyna Simoni; Mario Feola; Peter C Canizaro

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0003-2670)

Published

1991

Language

EN

Field

Chemistry (Physical Sciences)