Abstract
Summary
Extracts of human aortic intima were made in 0.9% NaCl and in 12% NaCl. Ultracentrifugally isolated human serum beta and alpha-2 lipoproteins were placed in similar salt concentrations. These were then examined in the immunoelectrophoresis system using antiserum against serum beta lipoprotein (which is equally effective against alpha-2 lipoprotein). Extract of aorta gave 2 lipoprotein arcs with this antiserum, one in the beta and one in the pre-albumin region, when prepared with 0.9% NaCl; there was only one arc (in the alpha-2 region) in extracts with 12% NaCl. This is interpreted as suggesting that serum alpha-2 lipoprotein is bound in the aortic intima in a pair of complexes both of which can be disrupted with strong salt solution.
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