Partial purification and characterization of the inherited Hl 1 and R 67 antigens of rabbit serum high density lipoprotein.
Purification and characterization of the Hl 1 antigen revealed a polypeptide with molecular weight of 20,000 by gel filtration. The peptide contained 20% neutral sugar and 4.5% neuraminic acid. Amino acid analysis as well as the N-terminal sequence for thirteen amino acid residues and three C-terminal amino acids were determined. Difference index analysis gave an indication that the Hl 1 polypeptide is unique. Purification of R 67 antigen did not give a pure polypeptide in sufficient amount to do chemical analysis. A crude fraction of R 67 antigen had three bands on SDS-PAGE, all with R 67 antigenic activity. The crude fraction contained 10% neutral sugar and 3.5% neuraminic acid. No N- or C-terminal amino acids could be determined for the crude fraction of R 67 antigen.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000941:Antigens / Q000235:genetics / Q000302:isolation & purification*; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D008075:Lipoproteins, HDL / Q000032:analysis / Q000276:immunology*; D008970:Molecular Weight; D011817:Rabbits
D000596:Amino Acids; D000941:Antigens; D002241:Carbohydrates; D008075:Lipoproteins, HDL