Characterization of the apolipoproteins of rat plasma lipoproteins.
Purified fractions of three major rat high-density lipoproteins (HDL) and one 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 molecular weight 27 000, appears to be homologous with the human A-I protein. However, rat HDL possesses two additional major components not reported in human HDL - an arginine-rich protein of molecular weight 35 000 and a protein of molecular weight 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 molecular weight appears similar or identical to the arginine-rich protein in rat HDL by every criterion employed for their characterization.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001053:Apolipoproteins / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D002850:Chromatography, Gel; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D008075:Lipoproteins, HDL / Q000032:analysis / Q000097:blood*; D008079:Lipoproteins, VLDL / Q000032:analysis / Q000097:blood*; D008970:Molecular Weight; D011487:Protein Conformation; D051381:Rats
D000596:Amino Acids; D001053:Apolipoproteins; D000939:Epitopes; D008075:Lipoproteins, HDL; D008079:Lipoproteins, VLDL