Abstract
The interaction of galactose oxidase with native and desialylated glycophorin A was studies by oxidizing human erythrocytes and globoside/phospholipid vesicles with the enzyme. Oxidation of the glycolipid was improved in the presence of vesicle-incorporationted glycophorin A. Although galactose oxidase is a very basic protein, it was not adsorbed on native human erythrocytes. Instead, neuraminidase-treated cells bound a substantial amount of galactose oxidase, but the enzyme seemed to be released into the buffer when desialylated glycoproteins had been oxidized.
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