Lorentz K, Flatter B, Kolle F W
J Clin Chem Clin Biochem. 1979 Nov;17(11):757-65.
Lectins from Canavalia ensiformis, Phaseolus vulgaris, and Triticum vulgare react with arylamidase, alkaline phosphatase, gamma-glutamyltransferase, and cholinesterase of human sera by formation of enzymatically active, mostly insoluble complexes. Arylamidase, alkaline phosphatase, and cholinesterase react more intensely in sera of healthy people than in sera of patients with liver and neoplastic diseases. Arylesterase is bound to a distinct degree only by concanavalin A. The enzymes mentioned above also react slightly with the following lectins in order of decreasing intensity: Ricinus communis, Arachis hypogaea, Helix pomatia, Glycine max, Dolichos biflorus, and Ulex europaeus. Though multiple forms containing less sialic acid are favourably bound, preincubation with neuraminidase does not improve the reaction except with soybean lectin. Since higher concentrations of lectins react also with fast moving fractions of high sialic acid content, no steric hindrance of the binding between lectins and sialoenzymes is supposed, as concluded from determination of the total enzyme activity.
来自刀豆、菜豆和小麦的凝集素通过形成酶活性的、大多不溶性复合物与人血清中的芳基酰胺酶、碱性磷酸酶、γ-谷氨酰转移酶和胆碱酯酶发生反应。芳基酰胺酶、碱性磷酸酶和胆碱酯酶在健康人血清中的反应比在患有肝脏疾病和肿瘤疾病患者的血清中更强烈。芳基酯酶仅与伴刀豆球蛋白A有不同程度的结合。上述酶与以下凝集素也有轻微反应，反应强度递减顺序为：蓖麻、花生、苹果蜗牛、大豆、双花扁豆和荆豆。尽管含较少唾液酸的多种形式更易结合，但除大豆凝集素外，用神经氨酸酶预孵育并不能改善反应。由于较高浓度的凝集素也与高唾液酸含量的快速移动组分发生反应，从总酶活性的测定得出结论，推测凝集素与唾液酸酶之间的结合不存在空间位阻。
