Abe H, Young M E, Moscarello M A, Sturgess J M
Cytobios. 1976;17(65):7-15.
Binding of Concanavalin A to the Golgi complex and the resultant effect on intramembrane particles and enzyme activity has been studied with Golgi-rich fractions isolated from rat liver. Con A binds mainly to the tubular network of the Golgi complex and, to a lesser extent, the peripheral regions of the cisternae. Interaction of Con A with Golgi membranes is accompanied by aggregation of intramembrane particles reflecting increased membrane fluidity. Enhancement of galactosyl transferase, membrane bound in the Golgi complex, also occurs with Con A binding.
已利用从大鼠肝脏分离出的富含高尔基体的组分，研究了伴刀豆球蛋白A与高尔基体复合物的结合以及对膜内颗粒和酶活性的最终影响。伴刀豆球蛋白A主要与高尔基体复合物的管状网络结合，在较小程度上也与扁平囊泡的周边区域结合。伴刀豆球蛋白A与高尔基体膜的相互作用伴随着膜内颗粒的聚集，这反映出膜流动性增加。伴刀豆球蛋白A结合还会使高尔基体复合物中膜结合的半乳糖基转移酶活性增强。
