Which Hgb is a β-δ chain hybrid that behaves similarly to Hgb S at pH 8.6?

Hemoglobin Lepore is a hybrid hemoglobin that results from a gene fusion of the beta and delta globin chains. This unique structure means that it will exhibit properties that are intermediate between the normal development of hemoglobin and the presence of hemoglobin S (which is characteristic of sickle cell disease).

At a pH of 8.6, hemoglobin Lepore migrates similarly to hemoglobin S during electrophoresis, due to the similarities in their structure and charge. This is significant in clinical diagnostics, as it may lead to misidentification if testing methods do not adequately differentiate between these two types of hemoglobin. The hybrid nature of hemoglobin Lepore enables it to present certain characteristics of hemoglobin S, such as altered solubility and analogous electrophoretic behavior, which is crucial for understanding both its clinical implications and the patient's hematological profile.

Other hemoglobins listed, such as hemoglobin CHarlem, GPhiladelphia, or DPunjab, do not have the same structural configuration or behavior at alkaline pH levels, thus making them distinct from hemoglobin Lepore in terms of their characteristics observed in clinical evaluations.