蚕豆凝集素的分离纯化和性质研究

蚕豆凝集素的分离纯化和性质研究 A STUDY ON ISOLATION AND PARTIAL CHARACTERIZATION OF A LECTIN FROM VICIA FABA 刘殿功 Liu Diangong Mei Lianqing Wu Chuanjing 1 first-author 梅连青 1 吴传京 1 武汉大学生物系 武汉大学生物系 Department of Biology, Wuhan University Department of Biology, Wuhan University 本文报导以武昌产蚕豆为材料,经抽提,分离纯化而得到高纯度的蚕豆凝集素VFL),经PAGE后,用考马斯亮兰液染色呈一条谱带,用高碘酸—Schiff试液染色呈阳性反应。用Bio-Gel P-100凝胶层析测定出VFL的表观分子量为46 000左右,经SDS—PAGE和6M盐酸胍—Sepharose 6B凝胶过滤测定,VFL的亚基分子量为23 600。VFL完整分子可能是由两个相同或相近的亚基组成。用凝胶电聚焦祛测定VFL的PI值为6.25。用DNS—Cl法和高压液相测定VFL的N-末端氨基酸为亮氨酸。VFL对兔红细胞、人的四种血型红细胞均有凝集作用,但对AB型红细胞凝集作用较弱。 The lectin from Vicia faba was extracted with phosphate buffered saline at 4℃, was isolated and purified by affinity chromatogrephy on SephadexG- 100, Electrophoresis of the purified lectin in pH8.3 buffer gave a one band （pattern） when the gels were stained with Cooma ssie blue or periodic acid-Schiff reagent, The active lectin is a glycoprotein with molecular weight of 46 600. This lectin molecule is possibly composed of two types of apparently identical subunits. This subunit had mol. wt 23 600. Isoeleetric separation of the purified lectin in polyacrylamide gel determined isoelectric point is pH 6.25. It’s major composition has the same N-terminal amino acid （Leucine）. VFL was agglutination active against all four types of human Erythrocytes and rabbit Erythrocytes. 蚕豆凝集素 糖蛋白 血红细胞凝集作用 亲和层析 电泳 vicia faba lectin glucoprotein hemagglutination affinity chromatography electrophoresis 1989-02-01 2021-04-01 2