Abstract: According to the ice-binding characteristic, antifreeze proteins in the leaves of Ligustrum lucidum were isolated by adsorption to ice pieces at 0°C. Using Sephadex G-100 gel filtration and DEAE cellulose-52 anion exchange chromatography, we obtained 4 protein fractions, including a 36 kDa protein, identified as antifreeze proteins by differential scanning calorimetry. The THA value of the protein was approximately 0.678 °C when the protein concentration was 5 mg.mL-1. The maximal absorption peak was 975 nm after full-spectrum scanning from 200 to 1 000 nm. The content of hydrophilic amino acids was relatively higher than that of the other proteins.