Characterization of the apolipoproteins of rat plasma lipoproteins

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Abstract
Purified fractions of 3 major rat high-density lipoproteins (HDL) and 1 rat very low-density lipoprotein (VLDL) were isolated by Sephadex gel chromatography or preparative sodium dodecyl sulfate gel electrophoresis. These proteins were characterized by amino acid analysis, end-group analysis, molecular-weight determination, polyacrylamide gel electrophoresis and circular dichroism. One of these rat proteins, of MW 27,000, appears to be homologous with the human A-I [apolipoprotein I] protein. Rat HDL possesses 2 additional major components not reported in human HDL, an arginine-rich protein of MW 35,000 and a protein of MW 46,000. The arginine-rich protein of the rat is similar in size and amino acid analysis to the arginine-rich protein reported in human VLDL. A major component of rat VLDL of 35,000 MW appears similar or identical to the arginine-rich protein in rat HDL by every criterion employed for their characterization.