What hemoglobin is a beta-delta chain hybrid and migrates to the same position as Hgb S at pH of 8.6?

Hemoglobin Lepore is indeed a beta-delta chain hybrid, and its unique structure is what allows it to migrate to the same position as Hemoglobin S (Hgb S) on electrophoresis at a pH of 8.6.

At this pH, hemoglobins are separated based on their charge; since both Hgb S and Hemoglobin Lepore contain similar charged properties, they exhibit similar migration patterns during electrophoresis. Hemoglobin Lepore is a product of a genetic deletion that results in an abnormal fusion of the beta and delta chains, leading to its distinct electrophoretic behavior. Understanding the structural consequences of chain fusions is critical, as it impacts not only the migration patterns seen in laboratory settings but also the overall function and stability of the hemoglobin molecule in physiological conditions.

In contrast, other hemoglobins, such as Hemoglobin A, Hemoglobin F, and Hemoglobin C, have different chain compositions and properties that impact their migration. Hemoglobin A consists of two alpha and two beta chains, Hemoglobin F has two alpha and two gamma chains, and Hemoglobin C is characterized by a mutation in the beta chain. This variation among the hemoglobins results in differing electrophoretic behaviors compared