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一种女贞叶抗冻蛋白的分离纯化
引用本文:刘尚 廖祥儒 张建国 苗会娟. 一种女贞叶抗冻蛋白的分离纯化[J]. 植物学报, 2007, 24(4): 505-510
作者姓名:刘尚 廖祥儒 张建国 苗会娟
作者单位:江南大学生物工程学院教育部工业生物技术重点实验室, 无锡 214122
摘    要:根据抗冻蛋白与冰结合的特性, 利用碎冰从女贞(Ligustrum lucidum)叶提取液中分离出抗冻蛋白。结果表明, 通过碎冰吸附、凝胶过滤和离子交换层析可以获得4个组分的蛋白质, 其中的1个经鉴定具有热滞活性。在蛋白质浓度为5 mg.mL-1时, 它的热滞活性(thermal hysteresis activity, THA)值为0.678°C, 对其进行全波长扫描(200-1 000 nm)发现在975nm处有吸收峰; 该蛋白亲水性氨基酸含量较高。

关 键 词:抗冻蛋白  性质  冰结合  女贞  纯化
收稿时间:2007-01-05
修稿时间:2007-01-18

Purification of an Antifreeze Protein from Ligustrum lucidum Leaves and Its Partial Characteristics
Shang Liu Xiangru Liao Jianguo Zhang Huijuan Miao. Purification of an Antifreeze Protein from Ligustrum lucidum Leaves and Its Partial Characteristics[J]. Bulletin of Botany, 2007, 24(4): 505-510
Authors:Shang Liu Xiangru Liao Jianguo Zhang Huijuan Miao
Affiliation:Educational Ministry Key Laboratary of Industrial Biotechnology, School of Biotechnology, Southern Yangtze University, Wuxi 214122, China
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.
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