Affiliation:
1. From the Department of Virus Research, Karolinska Institute School of Medicine, and the Department of Immunology, National Bacteriological Laboratory, Stockholm 1, Sweden
Abstract
Electron micrographs of isolated human α2M-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 α2M particles were 170 A and 100 A, respectively. Purified rabbit αmacroglobulins contained about 80% α1M- and 20% α2M-globulins. The isolated rabbit α1M- and α2M-molecules were morphologically indistinguishable from one another and from human α2M-molecules.
Preliminary immunoprecipitation studies demonstrated that the two rabbit αM-globulins were antigenically different. Sedimentation constant determinations gave s20, w values of 18.8 and 18.2 for rabbit α1M and α2M, respectively.
Publisher
Rockefeller University Press
Subject
Immunology,Immunology and Allergy
Cited by
50 articles.
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