Lectin-like activity of lupin seed conglutin γ, a glycoprotein previously referred to as a storage protein

Abstract
The lupin seed glycoprotein conglutin γ was capable of binding various exogenous and endogenous N-glycosylated proteins and also specifically bound to a Sephadex G-75 column. The binding activity of conglutin γ was abolished by either addition of 10 mM EDTA or by enzymic deglycosylation and acid treatment. In the latter case activity could be restored by the addition of Mn and Ca ions. Immunological homology at polypeptide level of conglutin γ with other legume lectins was found.

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