Microcomplement fixation and particle size of chicken lipoproteins.
Conformational changes of the lipoproteins of chicken serum and egg yolk were studied with the use of microcomplement fixation. Egg yolk very low density lipoproteins and serum total low density lipoproteins were separated by 2% agarose gel chromatography into four and five fractions, respectively, with different average particle diameters. A correlation between percent complement fixed at equivalence and particle diameter was noted. Thus, smaller particles fixed less complement. The shortening of the radius of curvature could alter the steric fit of apolipoprotein with antibody and, as a consequence, reduce complement fixation. The patterns obtained after delipidation of very low density lipoproteins indicate a general distortion of apolipoprotein conformation supporting the view that lipids are essential for maintaining the conformation of these apolipoproteins. On the other hand, the general conformation of the high density apolipoproteins does not appear to depend on lipid content. It has been reported that lipids restrain the free movement of these apolipoproteins. After delipidation, the greater degree of freedom allowed the apolipoprotein may increase the strength of the antigen-antibody union and therefore an increase in complement fixation is observed. These studies demonstrate the applicability of quantitative microcomplement fixation to the eludication of lipoprotein structure and function.