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洋紫荆凝集素的分离纯化和性质
引用本文:彭建宗,陈兆平,程双奇. 洋紫荆凝集素的分离纯化和性质[J]. 植物学通报, 2000, 17(3): 266-269
作者姓名:彭建宗  陈兆平  程双奇
作者单位:华南师范大学生物系!广州510631
摘    要:利用酸化处理的Sepharose 6B亲和柱从洋紫荆种子中分离纯化出了洋紫荆凝集素(BVL),其比活性比抽提液提高了159倍,活力回收率为49.0%。BVL分子量为81000,由两个相同的亚基组成。等电聚焦凝胶电注测得其等电点为4.95。其紫外吸收高峰在276nm处。BVL具一定的的热稳定性和酸碱稳定性。N-乙酰-D氨基半乳能强烈地抑制BVL对兔红细胞的凝集作用。乳糖、半乳糖也有较强的抑制定性。N

关 键 词:凝集素 洋紫荆 亲和层析 纯化 理化性质
修稿时间:1999-04-01

Purificationand Characterization of Lectin from Bauhinia variegata L.
PENG Jian-Zong CHEN Zhao-Ping CHENG Shuang-Qi. Purificationand Characterization of Lectin from Bauhinia variegata L.[J]. Chinese Bulletin of Botany, 2000, 17(3): 266-269
Authors:PENG Jian-Zong CHEN Zhao-Ping CHENG Shuang-Qi
Abstract:Bauhinia variegata lectin(BVL) has been purified from the seed of Bauhinia variegata L. by affinity c hromatography on an acid-treated Sepharose 6B column . The hemagglutinating act ivity of the purified BVL increased 159 times and the activity recovery is 49.0 %. The molecular weight is 81 000 and the molecule consists of two identical sub units. Its isoelectric point is 4.95. N-acetyl-D-galactosamine is the most p otent inhibitors of BVL. Lactose and galactose can also inhibit the agglutinati on of rabbit erythocytes by BVL.
Keywords:Lectin  Bauhinia variegata  Aff inity chromatography  Purification  
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