The hyperactivity of hamster fibroblast lysosomal enzymes after endocytosis of sucrose.

The sialoglycoproteins of the human erythrocyte membrane can be separated into at least eight periodic acid Schiff-positive components using sodium dodecyl sulfate gel electrophoresis in the discontinuous buffer system of Laemmli. All eight components can also be labeled by mild periodate oxidation followed by reduction with NaB³H₄. Periodic acid Schiff 2 can be resolved into at least three distinct components. Two sialoglycoproteins, with apparent molecular weights of 35,000 and 27,000 do not appear to be labeled by lactoperoxidase-catalyzed iodination at the external membrane surface.