Purification and molecular properties of acid phosphatase from sycamore cell walls

Abstract

Abstract. An acid phosphatase is isolated and purified to homogeneity from sycamore cell walls. The enzyme, which has a molecular weight close to 100,000, is a glycoprotein and is most probably made up of one polypeptide chain only. Its amino acid composition has been determined. Although homogeneous to polyacrylamide gel electrophoresis under non‐denaturing conditions, the enzyme preparation still contains protease traces that tend to split polypeptide chain in two fragments.