Which isoenzyme of ALP migrates the farthest toward the anode during electrophoresis at pH 8.6?

The isoenzyme of alkalin phosphatase (ALP) that migrates the farthest toward the anode during electrophoresis at pH 8.6 is the liver ALP. This is primarily due to its unique biochemical properties, specifically its charge and size relative to the other isoenzymes. At a neutral to slightly alkaline pH, such as 8.6, the liver ALP has a higher negative charge compared to the other isoenzymes.

When subjected to an electric field during electrophoresis, molecules migrate based on their charge and size. The liver ALP possesses a more pronounced negative charge, which causes it to move toward the positively charged anode more rapidly than the other isoenzymes, such as bone, renal, or intestinal ALP, which have different properties. This distinct migration pattern is essential for differentiating various isoenzymes in clinical laboratory settings, helping to indicate specific diseases affecting the liver.