Which isoenzyme of ALP migrates the farthest towards the anode at pH 8.6?

The isoenzyme of alkaline phosphatase (ALP) that migrates the farthest towards the anode at pH 8.6 is the liver isoenzyme. Each isoenzyme has a unique charge and structure, which influences its migration during electrophoresis. At a neutral to slightly alkaline pH, the liver isoenzyme exhibits a higher negative charge compared to the other isoenzymes, allowing it to migrate further towards the anode.

The liver isoenzyme is produced predominantly in the liver and is often used as a diagnostic marker for liver diseases. Its migration characteristics can be crucial for distinguishing between different causes of elevated ALP levels.

In contrast, the bone, intestinal, and placental isoenzymes each differ in their charge and structure, resulting in less movement towards the anode at this pH. The bone isoenzyme, for instance, has a different electrophoretic mobility due to its distinct biochemical composition and is less negatively charged compared to the liver isoenzyme. This variance in migration patterns is utilized in clinical settings to help identify the source of elevated alkaline phosphatase levels, aiding in the diagnosis of conditions related to different organs.