Affinity chromatography of lysosomal enzymes in plasma, urine and fibroblasts of patients with mucolipidosis (ML) II and III

Abstract

Using Concanavalin A Sepharose (Con A Sepharose), the elution pattern of plasma α- d-mannosidase, N- acetyl-β- d-glucosaminidase , acid phosphatase and α- l-fucosidase from patients with ML II and III was comparable to that of plasma of a normal individual. The elution of urinary N- acetyl-β- d-glucosaminidase and α- d-galactosidase was the same in mucolipidosis II as in normal controls. ML II patients' fibro blasts have a somewhat lower percentage elution of N- acetyl-β- d-glucosaminidase and acid phosphatase than do normal controls. Using a column of fucose-binding lectin, no activity could be found for eight lysosomal enzymes which were tested in the elution fractions of plasma from patients with mucolipidosis II and normal controls. Elution of seven plasma lysosomal enzymes was obtained using a galactosebinding lectin. No significant differences were noted between plasma of normal persons and patients with mucolipidosis II. Our results indicate that the lysosomal enzymes tested do not adsorb to fucose-binding lectin and that there are no profound differences in the elution of lysosomal enzymes from Con A Sepharose and galactose-binding lectin between normal persons and patients with ML II and ML III.