Abstract
Two procedures for separation of globin chains from hemoglobin by starch gel electrophoresis in 6 M urea in EDTA-borate-Tris buffer systems are described. The utility of the systems is demonstrated with comparisons to other approaches for analyzing hemoglobin chains (a) by characterizing the variant chain for several human hemoglobins using both hemolyzates and purified hemoglobins, (b) in determining the basis of the failure of canine chains to be resolved by the systems, (c) by deteeting probable nonheme proteins on CMC chromatograms of human globin chains, and (d) in characterizing certain "shadow" fractions as being generated from the major globin chains due to oxidation and/or carbamylation.
| Original language | English |
|---|---|
| Pages (from-to) | 312-330 |
| Number of pages | 19 |
| Journal | Analytical Biochemistry |
| Volume | 34 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 1970 |
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