PARTIAL PURIFICATION AND CHARACTERIZATION OF THE INHERITED H1 1 AND R 67 ANTIGENS OF RABBIT SERUM HIGH DENSITY LIPOPROTEIN

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Abstract
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.