English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

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 kDa 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 sulphate 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 Canavalia ensiformis lectin-Sepharose. The carbohydrate composition of the ceruloplasmin fractions was analysed. It is suggested that fucose might be a determinant for the microheterogeneity in the carbohydrate chains of ceruloplasmin.

Interactions of Purified Human Ceruloplasmin with Lathyrus odoratus, Lern culinaris and Canavalia ensiformis Lectins