Studies of the biochemical and immunological properties of human neutrophil alkaline phosphatase with comparison to the established alkaline phosphatase isoenzymes.

A range of affinity column chromatographic procedures and various inhibitors have been used to compare human neutrophil alkaline phosphatase with the three established isoenzymes. The column chromatography studies have clearly distinguished neutrophil alkaline phosphatase from the intestinal isoenzyme. Inhibition studies with L-phenylalanine, L-homoarginine and levamisole have revealed a distinct pattern of inhibition for liver, kidney and neutrophil alkaline phosphatase which is quite different from the pattern shown by placental and intestinal alkaline phosphatase. Immunospecificity experiments with a monoclonal antibody raised to human liver alkaline phosphatase have shown that it cross reacts with alkaline phosphatase from kidney, bone and neutrophil. In all studies, neutrophil alkaline phosphatase has virtually identical properties to that of liver, kidney and bone alkaline phosphatase. This is strong evidence that neutrophil alkaline phosphatase is a product of the same structural gene which codes for the liver/bone/kidney group of human alkaline phosphatases.