Abstract
The apoprotein moiety of human serum low density lipoprotein was separated by SDS-gel electrophoresis into several components ranging in molecular weight between approximately 80,000 and 10,000 daltons. Amino acid analyses and N-terminal determination were done on each fraction. Every fraction was found to have essentially identical amino acid composition. We interpret the data to indicate that apoLDL is an aggregate composed of a small number of fundamental subunits of similar amino acid composition.
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