大鼠α1-巨球蛋白高亲和力受体结合域的表达与重折叠
Expression and refolding of a high-affinity receptor binding domain from rat alpha 1-macroglobulin.
作者信息
Nielsen K L, Sottrup-Jensen L, Fey G H, Thøgersen H C
机构信息
Department of Chemistry, University of Arhus, Denmark.
出版信息
FEBS Lett. 1995 Oct 16;373(3):296-8. doi: 10.1016/0014-5793(95)01064-l.
A recombinant version of the receptor binding domain of rat alpha 1-macroglobulin (RBDv) consisting of residues 1319-1474 has been expressed in E. coli. Competition experiments with 125I-labelled methylamine treated human alpha 2-macroglobulin reveal that the alpha 1-macroglobulin-RBDv exhibit the same high affinity for the alpha 2-macroglobulin receptor as the entire 40 kDa light chain from rat alpha 1-macroglobulin. It is therefore concluded, that all determinants for receptor interaction reside in the C-terminal approx. 150 residues of the alpha-macroglobulin subunit.
由大鼠α1-巨球蛋白（RBDv）的1319 - 1474位残基组成的受体结合域的重组形式已在大肠杆菌中表达。用125I标记的甲胺处理的人α2-巨球蛋白进行的竞争实验表明，α1-巨球蛋白-RBDv对α2-巨球蛋白受体的亲和力与大鼠α1-巨球蛋白的整个40 kDa轻链相同。因此可以得出结论，受体相互作用的所有决定因素都位于α-巨球蛋白亚基的C末端约150个残基中。
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