Small‐Angle X‐Ray Scattering Study of the Interaction between Human α2‐Macroglobulin and Trypsin
- 3 March 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 122 (3) , 663-666
- https://doi.org/10.1111/j.1432-1033.1982.tb06489.x
Abstract
The interaction between human .alpha.2-macroglobulin and [bovine pancreas] trypsin yields a complex of 2-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 1st 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 2 sites, each of which is partly filled with 1 trypsin molecule.This publication has 24 references indexed in Scilit:
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