Chinese Bulletin of Botany ›› 2007, Vol. 24 ›› Issue (04): 505-510.
• 技术与方法 • Previous Articles Next Articles
Shang Liu Xiangru Liao Jianguo Zhang Huijuan Miao
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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.
Shang Liu Xiangru Liao Jianguo Zhang Huijuan Miao. Purification of an Antifreeze Protein from Ligustrum lucidum Leaves and Its Partial Characteristics[J]. Chinese Bulletin of Botany, 2007, 24(04): 505-510.
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