Kitagaki H, Seno N, Yamaguchi H, Matsumoto I
J Biochem. 1985 Mar;97(3):791-9. doi: 10.1093/oxfordjournals.jbchem.a135119.
An agglutinin of Clerodendron trichotomum fruit (CTA), found to be specific for N-acetyl-D-galactosamine and D-galactose, was isolated and characterized. The fruit extract was decolorized first by passage through a Toyopearl column and a phenyl-Sepharose column. Then the lectin activity was adsorbed on p-aminophenyl N-acetyl-alpha-D-galactosaminide- or p-aminophenyl beta-D-galactoside-Sepharose, and eluted as a sharp peak with 0.2 M lactose. The purified CTA was found to be homogeneous by SDS-polyacrylamide gel electrophoresis, gel chromatography and ultracentrifugal analysis, and was determined to be a glycoprotein homodimer with a molecular weight of 56,000 daltons. Hemagglutination-inhibition assay indicated that CTA is most specific for N-acetyl-D-galactosaminide with a hydrophobic aglycon.
一种海州常山果实凝集素（CTA）被分离并鉴定，它对N-乙酰-D-半乳糖胺和D-半乳糖具有特异性。果实提取物首先通过Toyopearl柱和苯基琼脂糖柱进行脱色。然后，凝集素活性吸附在对氨基苯基N-乙酰-α-D-半乳糖胺或对氨基苯基β-D-半乳糖苷琼脂糖上，并用0.2 M乳糖洗脱为尖锐峰。通过SDS-聚丙烯酰胺凝胶电泳、凝胶过滤色谱和超速离心分析发现纯化的CTA是均一的，并且被确定为分子量为56,000道尔顿的糖蛋白同二聚体。血凝抑制试验表明，CTA对具有疏水苷元的N-乙酰-D-半乳糖胺最具特异性。
