Tartrate-resistant (band 5) acid phosphatase activity measured by electrophoresis on acrylamide gel

Abstract

A tartrate-resistant acid phosphatase was isolated from a human spleen infiltrated with reticulum cells of leukemic reticuloendotheliosis. The purified enzyme was used to establish the optimal conditions for quantitative analysis of this enzyme by electrophoresis on acrylamide gel. As little as 0.1 unit of enzyme activity (or 1 ng of the purified enzyme protein) could be quantitatively detected when it was mixed with 4 mg of albumin before electrophoresis.