DETERMINATION OF LECTIN SUGAR DISSOCIATION-CONSTANTS BY AGAROSE AFFINITY ELECTROPHORESIS
DETERMINATION OF LECTIN SUGAR DISSOCIATION-CONSTANTS BY AGAROSE AFFINITY ELECTROPHORESIS
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DOI：
10.1016/0003-2697(86)90282-4
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发表时间：
1986-08-01
影响因子：
2.9
通讯作者：
MACKIEWICZ, S
中科院分区：
文献类型：
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作者：
MACKIEWICZ, A;MACKIEWICZ, S
琼脂糖交叉亲和电泳（aff-EP）测定凝集素-糖解离常数（Ki）。在aff-EP的第一维中，糖（α-EP）的量增加，甲基-D-甘露糖苷）加入到给定浓度的凝集素（伴刀豆球蛋白A）中。然后用α 1-酸性糖蛋白、α 1-抗胰蛋白酶和α-胰蛋白酶进行电泳。作为凝集素-糖相互作用的标志物。建立了确定凝集素-糖-糖蛋白相互作用机理和常数的数学方程。伴刀豆球蛋白A-α-的平均值根据引入的方程计算的甲基-D-甘露糖苷的解离常数为0.28 mM。在该系统中，它也可以确定凝集素-糖蛋白的解离常数（K）。观察到的糖凝集素-糖蛋白结合的影响可能是由于疏水相互作用，因为添加非离子去污剂引起这种现象的逆转。
Agarose crossed affinity electrophoresis (aff-EP) was employed for the determination of lectin-sugar dissociation constants (Ki). In the first dimension of the aff-EP increasing amounts of sugar (.alpha.-methyl-D-mannoside) were added to a given concentration of lectin (concanavalin A). Then the electrophoresis was run with .alpha.1-acid glycoprotein, .alpha.1-antitrypsin and .alpha.-fetoprotein as markers of lectin-sugar interactions. Mathematical equations for determination of the mechanisms and constants of lectin-sugar-glycoprotein interactions were developed. The mean value of the concanavalin A-.alpha.-methyl-D-mannoside dissociation constant calculated according to the introduced equations was 0.28 mM. In this system it was also possible to determine lectin-glycoprotein dissociation constants (K). The observed influence of the sugar on lectin-glycoprotein binding might be due to hydrophobic interactions since the addition of nonionic detergent caused reversal of this phenomenon.