Which hemoglobins migrate with hemoglobin C at pH 8.6?

Hemoglobin C is known for its unique characteristics and migration patterns during electrophoresis. At a pH of 8.6, hemoglobin C has a similar net charge to certain other hemoglobins, which causes them to migrate together in electrophoretic assays.

In this context, hemoglobin A2 and hemoglobin O (especially O Arab) do not share the same charge properties that would allow them to migrate with hemoglobin C at this pH. Hemoglobin A2 typically migrates differently due to its specific amino acid composition, and hemoglobin O varieties vary significantly in their migration patterns as well.

However, hemoglobin C Harlem is characterized by a specific mutation that can affect its charge in a way that allows it to co-migrate with hemoglobin C at this pH. The presence of hemoglobin A2 along with hemoglobin O and hemoglobin C Harlem is significant because they all exhibit the same charge characteristics that lead to concurrent migration on a gel.

Thus, the accuracy of the answer is due to the shared migration patterns of hemoglobin A2, hemoglobin O, and hemoglobin C Harlem at an alkaline pH, distinguishing them from other hemoglobin types that migrate differently under the same conditions.