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梨形环棱螺凝集素的初步研究
引用本文:张吉强,李清漪. 梨形环棱螺凝集素的初步研究[J]. 生物化学与生物物理进展, 1995, 22(3): 281-283
作者姓名:张吉强  李清漪
作者单位:第三军医大学组织胚胎学教研室;西南师范大学生物系
摘    要:通过Sepharose 4B-甲状腺球蛋白亲和层析,从梨形环棱螺Bellamya purificata体内分离到的一种凝集素,不连续PAGE显示其为单一的蛋白质谱带.它能凝集兔、猪、鸭等动物的红细胞,但不能凝集人的A、B、O及AB型血的红细胞和固定后的兔红细胞.其凝集活力可被1.0mol/L的乳糖、半乳糖和60g/L的甲状腺球蛋白抑制,但不能被碱性硼酸缓冲液抑制.对温度变化敏感,有较宽的最适pH范围.

关 键 词:梨形环棱螺   凝集素   理化性质   纯化
收稿时间:1994-04-25
修稿时间:1994-07-16

A Preliminary Study on Bellamy purificata Lectin
Zhang Jiqiang and Li Qingyi. A Preliminary Study on Bellamy purificata Lectin[J]. Progress In Biochemistry and Biophysics, 1995, 22(3): 281-283
Authors:Zhang Jiqiang and Li Qingyi
Affiliation:Third Military Medical College;Third Military Medical College
Abstract:By Sepharose 4B-thyroglobulin affinity column chromatography a lectin was purified from Bellamya purificata. It showed a single band on alkaline PAGE. This lectin (BPL) agglutinated red blood cells of rabbit,duck and pig,but not of human blood types or formalin and/or glutaraldehyde-fixed rabbit erythrocytes. Its agglutination activity could be inhibited by 1.0mol/L lactose or galactose as well as 60g/L thyroglobulin, but not by alkaline borate buffer.BPL was temperature-sensitive,while showed a broad optical pH range (pH4.56-9.96).
Keywords:Bellamya purificata   lectin   physicochemical characterization   purification
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