Alexander S S, Livingstone L R, Yates L D, Sage H J
Biochim Biophys Acta. 1978 Sep 22;512(2):350-64. doi: 10.1016/0005-2736(78)90259-6.
By sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis the plasma membranes from porcine lymphocytes contain at least 30--35 glycopolypeptides and one or more glycolipids to which one or more of 12 purified lectins bind. The specificities of binding generally followed the same pattern as those of the reaction of the lectin with intact pig lymphocytes. Some lectins (e.g., the isolectin pair, Agaricus bisporus lectins A and B and a group consisting of the Lens culinaris A and B isolectins and the closely related Pisum sativum lectins) bind to almost identical populations of plasma membrane components and compete with each other for all their binding sites. Others (e.g., Concanavalin A and the Lens culinaris-Pisum sativum group and a group consisting of phytohemagglutinin-L, Ricinus communis lectin-60 and Ricinus communis lectin-120 bind in a cross reactive manner to some common binding moieties but, in addition, to certain nonshared ones. Still others (e.g., soybean agglutinin, peanut agglutinin and wheat germ agglutinin) do not share any common binding moieties with the other lectins. The amount of lectin binding and the number of membrane components to which a lectin binds is directly related to the Ka of binding of the lectin to the intact lymphocyte. Those with high Ka (Cocanavalin A Lens culinaris lectins, Pisum sativum lectins, phytohemagglutinin-L), bind to 20-30 different components giving very complex binding patterns while those with lower Ka (Agaricus bisporus lectins, wheat germ agglutinin, peanut agglutinin, and soybean agglutinin) bind to 8--13 components with easily distinguishable patterns. Soybean agglutinin binds almost exclusively to a glycolipid fraction while for the others one or more glycopolypeptides served as the major lectin-binding molecule. The Ricinus lectins, two lymphocyte toxins, bind to essentially every plasma membrane component to which the mitogen phytohemagglutinin-L binds, in fact competing for most of those plasma membrane moieties which bind phytohemagglutinin-L.
通过十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳分析，猪淋巴细胞的质膜含有至少30 - 35种糖多肽和一种或多种糖脂，12种纯化凝集素中的一种或多种可与这些糖多肽和糖脂结合。凝集素结合的特异性通常与凝集素与完整猪淋巴细胞反应的特异性遵循相同模式。一些凝集素（例如，双孢蘑菇凝集素A和B这一同种凝集素对，以及由小扁豆凝集素A和B同种凝集素和密切相关的豌豆凝集素组成的一组凝集素）与几乎相同的质膜成分群体结合，并相互竞争所有结合位点。其他凝集素（例如，伴刀豆球蛋白A以及小扁豆 - 豌豆组，和由植物血凝素 - L、蓖麻凝集素 - 60和蓖麻凝集素 - 120组成的一组凝集素）以交叉反应的方式与一些共同的结合部分结合，但此外还与某些非共享部分结合。还有一些凝集素（例如，大豆凝集素、花生凝集素和麦胚凝集素）与其他凝集素没有任何共同的结合部分。凝集素结合的量以及凝集素结合的膜成分数量与凝集素与完整淋巴细胞结合的解离常数（Ka）直接相关。那些具有高Ka的凝集素（伴刀豆球蛋白A、小扁豆凝集素、豌豆凝集素、植物血凝素 - L）与20 - 30种不同成分结合，呈现非常复杂的结合模式，而那些具有较低Ka的凝集素（双孢蘑菇凝集素、麦胚凝集素、花生凝集素和大豆凝集素）与8 - 13种成分结合，具有易于区分的模式。大豆凝集素几乎只与糖脂部分结合，而对于其他凝集素，一种或多种糖多肽是主要的凝集素结合分子。两种淋巴细胞毒素蓖麻凝集素与有丝分裂原植物血凝素 - L结合的几乎每个质膜成分结合，实际上竞争大多数与植物血凝素 - L结合的质膜部分。
