Abstract
Summary
High-density lipoproteins, isolated from human serum, were delipidated, and the apoproteins, so obtained, were characterized both electrophoretically, using acid and alkaline buffer systems, and chemically by treatment with a variety of reagent thiols and disulfides and their combinations. The acid system was studied with and without 8 M urea. Depending on the electrophoretic system used, two or more components (polypeptides) were seen, presumably reflecting apoprotein aggregational differences under the several conditions of study.
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