论文部分内容阅读
用 0 .2 %SDS磷酸缓冲液从串珠镰刀菌 (Fusariummoniliforme)孢子表面抽提蛋白质。孢子表面蛋白经DEAE Sepharose阴离子交换柱层析和SephacrylS 10 0分子筛柱层析 ,分离和纯化了一种凝集素。该凝集素的分子量为 70kDa ,糖含量为 19.8% ,对兔血红细胞有很强的凝集活性 ,凝集活性被半乳糖特异性地抑制。EDTA和一些金属离子不影响凝集活性
Protein was extracted from the spore surface of Fusarium moniliforme with 0.2% SDS phosphate buffer. The spore surface protein was separated and purified by DEAE Sepharose anion exchange column chromatography and Sephacryl S100 column chromatography. The lectin has a molecular weight of 70 kDa and a sugar content of 19.8% and has strong agglutination activity on rabbit red blood cells. The agglutination activity is specifically inhibited by galactose. EDTA and some metal ions do not affect the agglutination activity