Biopolym. Cell. 1989; 5(1):51-57.
Structure and Function of Biopolymers
Interaction of human ceruloplasmin with Immobilized plant lectins
1Saenko E. L., 1Basevich V. V., 1Yaropolov A. I.
- A. N. Bakh Institute of Biochemistry, Academy of Sciences of the USSR
Moscow, USSR
Abstract
The specific binding of native and asialo human ceruloplasmin (CP) with immobilized plant lectins ConA, WGA, LCA and BS was investigated using P25-CP. The binding parameters were determined and interpreted. More than 100-fold difference in dissociation constants of native and deglycosylated CP complexes with ConA has permitted concluding that CP carbohydrate chains play the major role in binding with ConA. The dependences of parameters of CP binding with ConA on pH Ca2+-concentration were investigated and interpreted.
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