Bloth B, Chesebro B, Svehag S E
J Exp Med. 1968 Apr 1;127(4):749-56. doi: 10.1084/jem.127.4.749.
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.
通过负染色技术获得的分离的人α(2)M分子的电子显微镜照片显示，其形态结构均一，类似两个字母H和I组成的优美图案。α(2)M颗粒的长度和宽度的众数分别为170埃和100埃。纯化的兔α巨球蛋白含有约80%的α(1)M球蛋白和20%的α(2)M球蛋白。分离的兔α(1)M分子和α(2)M分子在形态上彼此无法区分，与人α(2)M分子也无法区分。初步免疫沉淀研究表明，两种兔αM球蛋白在抗原性上不同。沉降常数测定得出，兔α(1)M和α(2)M的s(20,w)值分别为18.8和18.2。
