At pH 8.6, which hemoglobin migrates to the same position as Hgb A2?

At a pH of 8.6, hemoglobin C (Hgb C) migrates to the same position as hemoglobin A2 (Hgb A2) during electrophoresis. This is significant because the charge and structure of hemoglobin molecules influence their migration patterns under these electrophoretic conditions. Hgb A2, which is common in adults, has a specific charge that aligns closely with Hgb C at alkaline pH levels.

Hgb C is a variant of hemoglobin that results from a mutation in the beta-globin gene, leading to alterations primarily in its structure and charge. At this pH, hemoglobin C does not migrate as far towards the anode as other variants like Hgb S or Hgb F. This is crucial for laboratory diagnosis, particularly in differentiating between various hemoglobinopathies.

Migration patterns at pH 8.6 have important implications for both clinical diagnostics and the understanding of hemoglobin variants, making the identification of such alignments vital for accurate assessments in hematology.