A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean pine (Pinus koraiensis) by a combination of anion exchange, hydrophobic interaction, and gel filtration chromatography. The protein is less abundant than vicilin in low-salt extracts of mature Korean pine seeds. SDS-PAGE analysis revealed that convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript. Similar to vicilin, native convicilin appeared to be homotrimeric. Circular dichroism (CD) and differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than pine vicilin. Its transition temperature was 75.57�C compared with 84.13�C for vicilin. The urea induced folding-unfolding equilibrium of pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41�0.15 M.

Purification and characterization of convicilin, a vicilin-like globulin, from Korean pine (<i>Pinus koraiensis</i>)

244th National Meeting (2012)

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Purification and characterization of convicilin, a vicilin-like globulin, from Korean pine (Pinus koraiensis)