Improved electrophoretic resolution of human serum alkaline phsophatase isoenzymes in agarose gel by Triton X-100.

Triton X-100 caused the liver isoenzymes of alkaline phosphatase in some serum samples to separate into two fractions on agarose gel electrophoresis. One of these fractions migrated at the rate of the original one, and one migrated more slowly. The latter fraction corresponded to a fast-moving component on electrophoresis in Cellogel and seems to be identical with a slowly moving isoenzyme in starch and polyacrylamide gel electrophoresis. The migration rates of the bone, placental, and intestinal isoenzymes were unaltered, but the fractions appeared sharper.