Freier T, Rüdiger H
Institut für Pharmazie und Lebensmittelchemie der Universität Würzburg.
Biol Chem Hoppe Seyler. 1987 Sep;368(9):1215-23. doi: 10.1515/bchm3.1987.368.2.1215.
The immobilized lectin from the lentil (Lens culinaris) specifically binds two fractions out of the L. culinaris seed globulins. Both fractions are displaced from the lectin at low pH values. In addition, fraction I fails to interact at high ionic strengths, and fraction II in the presence of glucose or other lectin-specific sugars. The behaviour in zonal isoelectric precipitation and electrophoretical patterns indicate that both fractions represent subpopulations of the storage proteins. The interaction as demonstrated by affinity chromatography is corroborated by nephelometry: If the dissolved proteins (lectin plus fraction I or fraction II) are mixed under proper conditions the solutions become turbid. An even more pronounced interaction is observed if the lectin is reacted with both fractions at the same time. Seed albumins able to interact with the immobilized lectin include the dissolved lectin and two glycosidases (alpha-mannosidase, alpha-galactosidase) all of which are located in the protein bodies. A third glycosidase (beta-galactosidase) from outside of the protein bodies does not bind to the lectin. The results are discussed in view of the possibility that lectins may serve as packaging aids for other proteins in the protein bodies.
来自小扁豆（兵豆）的固定化凝集素特异性结合兵豆种子球蛋白中的两个组分。在低pH值下，这两个组分都会从凝集素上解离下来。此外，组分I在高离子强度下不发生相互作用，而组分II在葡萄糖或其他凝集素特异性糖类存在时也不发生相互作用。区带电泳等电沉淀行为和电泳图谱表明，这两个组分均代表储存蛋白的亚群。亲和色谱所证明的相互作用通过比浊法得到证实：如果在适当条件下将溶解的蛋白质（凝集素加组分I或组分II）混合，溶液会变浑浊。如果凝集素同时与两个组分反应，则会观察到更明显的相互作用。能够与固定化凝集素相互作用的种子白蛋白包括溶解的凝集素和两种糖苷酶（α-甘露糖苷酶、α-半乳糖苷酶），它们都位于蛋白体中。来自蛋白体外部的第三种糖苷酶（β-半乳糖苷酶）不与凝集素结合。鉴于凝集素可能作为蛋白体中其他蛋白质的包装辅助物这一可能性，对结果进行了讨论。
