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大瓶螺凝集素的分离纯化及部分性质研究 被引量:4

Studies on the Purification and Properties of Ampullaria gigas Spix lectin
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摘要 大瓶螺蛋白腺经磷酸盐缓冲液抽提、硫酸铵分级沉淀、SephadexG-100和Sepharose4B凝胶过滤,可获得在不连续PAGE(pH4.3和pH8.9)上显示单一蛋白质染色带的大瓶螺凝集素(AGL).该凝集素对人血红细胞无血型专一性,但对A型血红细胞的凝集作用最强.AGL的血凝活力可被乳糖或半乳糖所抑制.AGL分子中的中性糖含量为0.24mg/mg蛋白质.用SDS-PAGE法测得其亚基分子量为15000,且只有一种亚基.AGL中Cys和Phe的含量较高,并较耐热. Ampullaria gigas Spix lectin has been purified hy extraction with PBS,ammonium sulfate fractionation and chromatography on Sephadex G-100 and Sepharose 4B column. The lectin showed one single band both on PAGE (pH4.3 and PH8. 9) and on SDS-PAGE. The result showed that the lectin has only one kind of subunit. The molecular weight of the subunit was 15 000 when SDS-PAGE method was used for molecular weight determination. AGL is a glycoprotein containing 0. 24 mg per mg protein. Amino acid composition analysis showed that there was a large percentage of cystein and phenylamine.AGL can agglutinate four types of human erythrocytes,but it gave the strongest hemagglutination against type A human red blood cells. The hemagglutinating activity can be inhibited by lactose or D-galatose. Stability experiments proved that AGL can endure high temperature treatment.
作者 江红 李清漪
出处 《生物化学杂志》 CSCD 1996年第3期352-356,共5页
关键词 软体动物 大瓶螺 凝集素 提纯 Lectin, Ampullaria gigas Spix lectin, Purification, Properties
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参考文献6

  • 1高翔,中山大学学报,1992年,1卷,86页
  • 2何忠效,电泳,1990年
  • 3曾和期,1989年
  • 4孙册,凝集素,1986年
  • 5朱广廉,植物生理通讯,1982年,2卷,43页
  • 6张龙翔,生化实验方法和技术,1981年

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