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中文摘要：
黄牛肝菌（Boletus fulvus）经生理盐水浸提、CM-Sepharose、DEAE-Sepharose及Sephacryl S-100分子筛层析后得到黄牛肝菌凝集素（BFL）.经SDS-PAGE电泳及Sephacryl S-100分子筛层析检测表明,所得的BFL是由两个分子量约15.8kDa、非二硫键相连的亚基组成的表观分子量为32kDa的二聚体.BFL可快速凝集兔血红细胞,其最低凝集浓度为3.9μg/mL;糖抑制试验表明,胃粘蛋白、甲状腺球蛋白、卵粘蛋白和卵清蛋白均可抑制BFL活性.当温度在70℃以下和pH值在6.0~9.8之间时,BFL凝血活性基本不变.然而当温度至90℃以上和在极端pH值下,BFL凝血活性减弱甚至完全丧失.不同浓度的脲和盐酸胍对BFL凝血活性的影响表明：随着变性剂浓度的增加,BFL的结构逐渐被破坏.
英文摘要：
Boletus fulvus lectin（BFL）was isolated from Boletus fulvus,by extraction,ion-exchange chromatography on CM-Sepharose and DEAE-Sepharose followed by gel filtration on Sephacryl S-100.BFL is a homodimer with apparent molecular mass of 32 kDa and composed of two 15.8kDa subunits that are held together by noncovalent interactions.BFL could agglutinate rabbit erythrocyte,and it exhibited strong hemagglutination activity to rabbit erythrocytes at the concentration 3.9μg/mL.The result of carbohydrate inhibition assay showed that the gastric mucin,thyroglobulin,ovomucoid and ovalbumin could inhibit the agglutinating activity of BFL.The hemagglutination activity of BFL was stable under 70℃ and in a pH range of 6.0~9.8,while it was weak when temperature was higher than90℃ and in extreme pH range.Effects of different concentrations of urea and GuHCl on the hemagglutination activity of BFL indicated the increase of denaturant concentration could destroy the structure of BFL gradually.
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