Isolation and characterization of lysosomal alpha-mannosidase of placental tissue

The acidic α-mannosidase was purified 4400-fold by affinity chromatography on Concavalin A-Sepharose and heat treatment at 65‡C in the presence of 1 mM zinc ion. The enzyme did not resolve into multiple forms as in the case of enzymes from human liver and human kidney. The pH optimum of the enzyme was 4.2 in citrate-phosphate buffer. The K_m value for p-nitrophenyl-α-D-mannose was 1.9 mM. The molecular weight of the enzyme determined by gel filtration was 300,000. The enzyme contained 10.6% neutral sugars.