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. 1968 Apr 1;127(4):749-56.
doi: 10.1084/jem.127.4.749.

Ultrastructural studies of human and rabbit alpha-M-globulins

B Bloth, B Chesebro, S E Svehag

Ultrastructural studies of human and rabbit alpha-M-globulins

B Bloth et al. J Exp Med. .

Abstract

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.

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