Branegård B, Osterberg R, Sjöberg B
Eur J Biochem. 1982 Mar 1;122(3):663-6. doi: 10.1111/j.1432-1033.1982.tb06489.x.
The interaction between human alpha 2-macroglobulin and trypsin yields a complex of two trypsin molecules and one alpha 2-macroglobulin molecule as the main product. This is indicated from small-angle X-ray titration measurements in 0.02 M Tris/HCl buffer of pH 7.40 containing 0.2 M NaCl and 5 mM EDTA. The radius of gyration for the complex was determined to be 7.1 nm. The complex formation coincides with a decrease in the first side maximum of the scattering curve for alpha 2-macroglobulin. A comparison of the experimental data with those calculated from various models indicates that the data are consistent with the scattering from a hollow cylinder containing two sites, each of which is partly filled with one trypsin molecule.
人α2-巨球蛋白与胰蛋白酶之间的相互作用产生了以两个胰蛋白酶分子和一个α2-巨球蛋白分子组成的复合物作为主要产物。这是通过在含有0.2 M氯化钠和5 mM乙二胺四乙酸的pH 7.40的0.02 M Tris/盐酸缓冲液中进行小角X射线滴定测量得出的。该复合物的回转半径测定为7.1纳米。复合物的形成与α2-巨球蛋白散射曲线第一个侧面最大值的降低相吻合。将实验数据与从各种模型计算得出的数据进行比较表明，这些数据与来自一个含有两个位点的空心圆柱体的散射一致，每个位点部分填充有一个胰蛋白酶分子。
