Purification and some properties of violet-colored acid phosphatase from spinach leaves.

Abstract

The violet-colored acid phosphatase was purified from leaves of spinach (Spinacia oleracea). The purified preparation was found to be homogeneous by electrophoresis and ultracentrifugation. Concentrated solution of the enzyme had an intense violet color with a broad absorption band between 410 nm and 700 nm. The peak was at around 530 nm. The molecular weight of the enzyme was approximately 92000. The enzyme was composed of two subunits of equal size and contained manganese. The result of staining of the enzyme in disc electrophoresis gel by periodic acid-Schiff reagent indicated that the enzyme was glycoprotein.