Oda Y, Minami K, Ichida S, Aonuma S
Eur J Biochem. 1987 Jun 1;165(2):297-302. doi: 10.1111/j.1432-1033.1987.tb11441.x.
Two agglutinins with different agglutinating activity exist in Tulipa gesneriana bulbs. One is the T. gesneriana lectin which agglutinates yeasts as reported previously [Oda, Y. and Minami, K. (1986) Eur. J. Biochem. 159, 239-245]. The other agglutinin is a new one which agglutinates animal erythrocytes and was purified from the tulip bulbs using affinity chromatography on thyroglobulin-Sepharose 4B. The agglutinin agglutinated mouse and rat erythrocytes at a minimum concentration of 2 micrograms/ml and 30 micrograms/ml respectively, but did not agglutinate erythrocytes from other animals and yeasts even at a concentration of 1000 micrograms/ml. The agglutinin appeared homogeneous by disc gel electrophoresis at pH 4.3 and gel filtration. Its relative molecular mass was determined by gel filtration to be approximately 40,000. It was suggested that the agglutinin was composed of two different subunits of 26 kDa and 14 kDa by sodium dodecyl sulfate/polyacrylamide gel electrophoresis analysis. Binding of radioiodinated agglutinin to mouse erythrocytes indicated that the presence of a high-affinity site with a dissociation constant of 2.00 X 10(-9) M. In inhibition experiments thyroglobulin glycopeptides were the most potent inhibitors; thyroglobulin was also a potent inhibitor. Orosomucoid and mucin showed weak inhibition. The other glycoproteins, glycopeptides and sugars examined showed no inhibition.
郁金香球茎中存在两种具有不同凝集活性的凝集素。一种是郁金香凝集素，如先前报道的那样，它能凝集酵母[小田洋，南健（1986年）《欧洲生物化学杂志》159卷，239 - 245页]。另一种凝集素是新发现的，它能凝集动物红细胞，通过甲状腺球蛋白 - 琼脂糖4B亲和层析从郁金香球茎中纯化得到。该凝集素凝集小鼠和大鼠红细胞的最低浓度分别为2微克/毫升和30微克/毫升，但即使在1000微克/毫升的浓度下也不能凝集其他动物的红细胞和酵母。在pH 4.3的圆盘凝胶电泳和凝胶过滤中，该凝集素呈现均一性。通过凝胶过滤测定其相对分子质量约为40,000。十二烷基硫酸钠/聚丙烯酰胺凝胶电泳分析表明，该凝集素由26 kDa和14 kDa的两种不同亚基组成。放射性碘化凝集素与小鼠红细胞的结合表明存在一个解离常数为2.00×10⁻⁹ M的高亲和力位点。在抑制实验中，甲状腺球蛋白糖肽是最有效的抑制剂；甲状腺球蛋白也是一种有效的抑制剂。血清类粘蛋白和粘蛋白表现出较弱的抑制作用。所检测的其他糖蛋白、糖肽和糖类均无抑制作用。
