Department of Agronomy and Range Science, University of California, Davis, California 95616.
Plant Physiol. 1982 Feb;69(2):379-84. doi: 10.1104/pp.69.2.379.
The Concanavalin A (Con A) binding capacity of plasma membranes isolated from meristematic and mature regions of four-day-old soybean (Glycine max L. Merr. cv. Wells) roots was compared. Con A binding was studied using a radiochemical assay with tritiated ((3)H)-Con A and by an electron microscope technique using Con A-ferritin (Con A-F). In both cases, plasma membranes isolated from meristematic tissue bound significantly more Con A than did corresponding membranes from mature tissue. The relative difference in reactivity, as determined by the two procedures, was approximately 49% ((3)H-Con A) and 46% (Con A-F). In contrast, K(m) values, determined from (3)H-Con A binding curves, were approximately the same, indicating that receptor sites on plasma membranes from both sources were qualitatively similar.Since Con A specifically interacts with saccharide-containing portions of membrane glycoproteins and/or glycolipids, the data suggests that there is a decrease in the concentration of those components in plasma membranes during development or that there are qualitative changes in the structure of their oligosaccharide side chains.
比较了从四天大豆(Glycine max L. Merr. cv. Wells)根的分生组织和成熟区域分离的质膜的伴刀豆球蛋白 A(Con A)结合能力。使用放射性化学测定法(带有氚标记的(3)H-Con A)和使用伴刀豆球蛋白铁蛋白(Con A-F)的电子显微镜技术研究了 Con A 结合。在这两种情况下,与成熟组织的相应膜相比,从分生组织分离的质膜结合的 Con A 明显更多。两种方法确定的反应性的相对差异约为 49%((3)H-Con A)和 46%(Con A-F)。相比之下,(3)H-Con A 结合曲线确定的 K(m) 值大致相同,表明来自两种来源的质膜上的受体位点在质量上是相似的。由于 Con A 特异性地与膜糖蛋白和/或糖脂中的含糖类部分相互作用,因此数据表明在发育过程中这些成分在质膜中的浓度降低,或者其寡糖侧链的结构发生了定性变化。