Ultrastructural studies of human and rabbit alpha-M-globulins.
Electron micrographs of isolated human alpha(2)M-molecules, obtained by the negative contrast technique, revealed morphologically homogenous structures resembling a graceful monogram of the two letters H and I. The modal values for the length and width of the alpha(2)M particles were 170 A and 100 A, respectively. Purified rabbit alphamacroglobulins contained about 80% alpha(1)M- and 20% alpha(2)M-globulins. The isolated rabbit alpha(1)M- and alpha(2)M-molecules were morphologically indistinguishable from one another and from human alpha(2)M-molecules. Preliminary immunoprecipitation studies demonstrated that the two rabbit alphaM-globulins were antigenically different. Sedimentation constant determinations gave s(20, w) values of 18.8 and 18.2 for rabbit alpha(1)M and alpha(2)M, respectively.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D008259:Macroglobulins / Q000032:analysis; D008854:Microscopy, Electron; D011817:Rabbits; D014461:Ultracentrifugation
D008259:Macroglobulins