Ultrastructural Studies of Clq and of the Interaction Between Membranes and Complement Proteins

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Abstract
Ultrastructural studies of human C1q have demonstrated the molecule to exist in two distinct forms. Svehag and Bloth have described the molecule to be composed of six subunits arranged in a disc-like form. Our studies suggest that the disc-like form of the native molecule constitutes a disc-like coil consisting of six subunits which is capable of unfolding to a rod-like structure with an identical number of subunits. Red cell antibody complement complexes were prepared at various intermediate stages throughout the complement sequence; stroma was prepared from each and examined ultrastructurally. In complexes prepared up to the EAC1,4,2,3 stage in which no lesions were seen, sections of the membranes demonstrated the “tram-line” appearance described for normal red cell membranes by Dourmashkin and Rosse. At the EAC1–5 stage, when lesions first became visible, the membranes seen in section had retained their dense linear appearance; however, they had increased in width from 100 to 250 Å.

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