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FAILURE OF GLUCOSE-BINDING LECTINS CON A AND LENTIL LECTIN TO IDENTIFY GLYCATION OF HAEMOGLOBIN

机译:葡萄糖结合的凝集素CON A和扁豆状蛋白的破坏,无法鉴定血红蛋白的糖化

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摘要

We have studied the interaction of Concanavalin A and Lentil Lectin with glycohaemoglobin by a nephelometric lectin-glycogen/dextran precipitation system and monitored the inhibitory effect of glycohaemoglobin on the precipitation. Although inhibitory effects were clearly demonstrated using simple sugars and transferrin, no effect was observed by glycohaemoglobin in relevant concentrations, This is compared to affinity chromatography, binding studies using gel filtration and electrophoresis, and affinity studies using Concanavalin A immobilised on magnetisable polymer particles, Lack of interaction between glycohaemoglobin and lectins is discussed in view of steric constraints and reduced availability of the glycated residues and the stereochemical form of the glycated 1-amino-1-deoxy-fnlctosyl residues in glycohaemoglobin. [References: 26]
机译:我们已经通过比浊法凝集素-糖原/葡聚糖沉淀系统研究了伴刀豆球蛋白A和扁豆凝集素与糖血红蛋白的相互作用,并监测了糖血红蛋白对沉淀的抑制作用。尽管使用单糖和转铁蛋白已清楚地显示了抑制作用,但糖血红蛋白在相关浓度下未观察到任何作用。将其与亲和层析,使用凝胶过滤和电泳的结合研究以及使用固定在可磁化聚合物颗粒上的伴刀豆球蛋白A进行的亲和研究进行了比较鉴于空间限制和糖化血红蛋白中糖化的1-氨基-1-脱氧-芬太糖基残基的立体化学形式的空间限制和糖化残基的减少,讨论了糖化血红蛋白与凝集素之间的相互作用。 [参考:26]

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