真核生物核糖体拥有伴刀豆球蛋白A的结合位点。
Eukaryote ribosomes possess a binding site for concanavalin A.
作者信息
Howard G A, Schnebli H P
出版信息
Proc Natl Acad Sci U S A. 1977 Mar;74(3):818-21. doi: 10.1073/pnas.74.3.818.
Ribosomes prepared from chicken liver or rabbit reticulocytes bound concanavalin A in a molar ratio of approximately 1:1. This binding is to the large subunit of the eukaryote ribosomes with a dissociation constant of 5 X 10(-7) M (0 degrees). The binding of concanavalin A to Escherichia coli ribosomes was much less. Binding to the RNA or to possible membrane contaminants was ruled out in control experiments. Chicken liver ribosomes were labeled in vivo with 3H-labeled amino acids, purified, and dissociated in sodium dodecyl sulfate. Affinity chromatography of this preparation made it possible to isolate the small proportion of the ribosomal proteins (about 1.5%) containing the concanavalin A binding site. This protein moved as a single band during electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate and showed an apparent molecular weight of 31,000.
从鸡肝或兔网织红细胞制备的核糖体以大约1:1的摩尔比结合伴刀豆球蛋白A。这种结合发生在真核生物核糖体的大亚基上，解离常数为5×10⁻⁷ M（0摄氏度）。伴刀豆球蛋白A与大肠杆菌核糖体的结合要少得多。对照实验排除了其与RNA或可能的膜污染物的结合。鸡肝核糖体在体内用³H标记的氨基酸进行标记，纯化后在十二烷基硫酸钠中解离。对该制剂进行亲和层析，使得能够分离出含有伴刀豆球蛋白A结合位点的一小部分核糖体蛋白（约1.5%）。这种蛋白质在含有十二烷基硫酸钠的聚丙烯酰胺凝胶上电泳时呈现为单一的条带，表观分子量为31,000。
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