Which protein migrates in the β region at pH 8.6?

Transferrin is the protein that migrates in the β region at pH 8.6 during electrophoresis. This migration pattern is a result of its charge and size under the specified pH conditions. At pH 8.6, transferrin is negatively charged, allowing it to move toward the anode in an electric field, placing it in the β region of the electrophoretic gel.

Additionally, transferrin plays a crucial role in iron transport in the bloodstream, binding to iron ions and delivering them to various cells. Understanding its migration pattern can help in diagnosing conditions related to iron metabolism, such as iron deficiency anemia or hemochromatosis.

Other proteins listed have different characteristics that affect their migration patterns. For instance, haptoglobin is usually found in the α region, orosomucoprotein is characterized by its unique charge and size that would cause it to migrate differently, and antichymotrypsin migrates in the α region as well, primarily due to its structure and charge at that pH. This understanding of protein behavior under electrophoresis is essential in clinical chemistry for diagnosing various health conditions.