John Innes Institute, Colney Lane, NR4 7UH, Norwich, U.K..
Planta. 1977 Jan;136(3):253-9. doi: 10.1007/BF00385993.
The binding of a colloidal gold-Concanavalin A (ConA) complex to the plasmalemma of tobacco leaf protoplasts has been investigated using scanning electron microscopy. At 5° C the particles of gold-ConA appear to be randomly distributed over the surface of the protoplast. If the temperature is raised, the particles associate into clusters. Saturation of the membrane with particles can only occur when the weight of ConA in solution exceeds 1 μg/10(4) protoplasts in suspension, and when its concentration exceeds 15 μg/ml. These results are discussed in terms of the properties of the ConA binding site and the mobility of such sites within the membrane surface.
使用扫描电子显微镜研究了胶体金-伴刀豆球蛋白 A(ConA)复合物与烟草叶原生质体质膜的结合。在 5°C 时,金-ConA 颗粒似乎随机分布在原生质体表面。如果温度升高,颗粒会聚集在一起。只有当溶液中 ConA 的重量超过悬浮的 10(4)个原生质体 1 μg 时,并且当其浓度超过 15 μg/ml 时,膜上的颗粒才能达到饱和。这些结果是根据 ConA 结合位点的性质以及膜表面上这些位点的流动性来讨论的。