Abstract
A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean pine 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 isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean 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.
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