Interactions of Purified Human Ceruloplasmin withLathyrus odoratus, Lern culinarisandCanavalia ensiformisLectins

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Abstract
Human ceruloplasmin was isolated from normal serum by fractional polyethylene glycol precipitation and subsequent ion-exchange chromatography. The molecular mass determined by ultracentrifugation was 132 kilodalton, and an optical density ratio (A610/A280) of 0.046 was observed in the preparation. Immunoelectrophoresis, agarose-gel electrophoresis and N-terminal amino acid sequence analyses showed that the ceruloplasmin preparation was highly purified, while dodecyl sulfate polyacrylamide-gel electrophoresis indicated some degradation of the protein. Affinity chromatography showed that only a fraction of ceruloplasmin was bound to Lens culinaris or Lathyrus odoratus lectin-Sepharose, whereas nearly all the protein was bound to C. ensiformis lectin-Sepharose. The carbohydrate composition of the ceruloplasmin fractions was analyzed. Fucose might be a determinant for the microheterogeneity in the carbohydrate chains of ceruloplasmin.

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