Image processing of electron micrographs of human alpha2-macroglobulin half-molecules induced by Cd2+

Abstract

Human alpha2-macroglobulin is a tetrameric plasma inhibitor of proteinases. Its dissociation of Cd2+ gives functional dimers. Electron microscopy of negatively stained dimers shows their round-ended cylindrical shape with furrows delimiting 3 main stain-excluding domains. Image processing of electron micrographs shows the existence of 2 main orientations of the dimers on the carbon support film. The dimer is composed of 2 curved monomers linked in a central domain, and related by a 90.degree. rotation. Taking into account the known primary structure of alpha2-macroglobulin and the linkage of the 2 constitutive monomers by 2 disulfide bonds, the molecular organization of the dimer is discussed, extended to the tetrameric molecule and compared to the published models of human alpha2-macroglobulin.