How does Hgb C migrate in relation to Hgb A during electrophoresis on citrate agar?

Hemoglobin C (Hgb C) is a variant of normal hemoglobin (Hgb A) that results from a mutation in the beta-globin chain. During electrophoresis on citrate agar, Hgb C migrates slower than Hgb A due to its altered charge and structure.

In normal electrophoresis, hemoglobins are separated based on their size and net charge. Hgb A has a negative charge and moves toward the anode in an electric field, while Hgb C has a more significant positive shift in its charge compared to Hgb A. Consequently, this increased positivity means that Hgb C will not migrate as far toward the anode as Hgb A, resulting in slower migration. Therefore, the distinction in migration patterns allows for easy identification of various hemoglobin types in a clinical laboratory setting.