大豆凝集素与纯化的糖缀合物及大豆种子成分的相互作用。
Interactions of soya-bean agglutinin with purified glycoconjugates and soya-bean seed components.
作者信息
Bond H M, Chaplin M F, Bowles D J
出版信息
Biochem J. 1985 May 15;228(1):127-36. doi: 10.1042/bj2280127.
Abstract
A radioaffinity assay for lectin binding to receptors was developed and characterized by using the interactions between soya-bean agglutinin and four glycoconjugates, namely thyroglobulin, galactomannan, fetuin and asialofetuin. On application of the assay to soya-bean extracts a wide range of seed components were found to have the capacity to interact with soya-bean agglutinin. These included both trichloroacetic acid-soluble and trichloroacetic acid-insoluble glycoconjugates and two classes of particulate matter distinguished by their differential solubility in Triton X-100.
摘要
通过利用大豆凝集素与四种糖缀合物（即甲状腺球蛋白、半乳甘露聚糖、胎球蛋白和去唾液酸胎球蛋白）之间的相互作用，开发并表征了一种用于凝集素与受体结合的放射亲和测定法。将该测定法应用于大豆提取物时，发现多种种子成分具有与大豆凝集素相互作用的能力。这些成分包括三氯乙酸可溶和三氯乙酸不溶的糖缀合物，以及两类根据其在 Triton X-100 中的不同溶解度区分的颗粒物。
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