Abstract
The pre-α-lipoprotein of human serum observed by electrophoresis on agarose gel had mobility and staining characteristics similar to those of albumin. The high lysolecithin and free fatty acid content of this fraction and the ability of albumin to bind these lipids further support the hypothesis that pre-α-lipoprotein is albumin. The presence of large relative amounts of other phospholipids as well as neutral lipids in the pre-α-lipoprotein fraction, however, along with the immunodiffusion studies, suggests that lipoprotein other than albumin resides in the pre-α-lipoprotein fraction. Such lipoprotein does not appear to be a β-lipoprotein or an extension of the α-lipoprotein into the pre-α-lipoprotein fraction.
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