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Biologic and chemical characterization of hla antigens in human-serum

Academic Article
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Overview

authors

  • Allison, J. P.
  • Pellegrino, M. A.
  • Ferrone, S.
  • Callahan, G. N.
  • Reisfeld, Ralph

publication date

  • 1977

journal

  • Journal of Immunology  Journal

abstract

  • HLA antigens of both the A and B loci were shown to be associated with the high density lipoprotein fraction of serum prepared by ultracentrifugal flotation. HLA-A9 antigens were purified 100-fold with essentially complete recovery by a simple procedure of high density lipoprotein preparation involving precipitation with polyanions and ultracentrifugal flotation. The purified lipid-associated antigen was immunogenic since it elicited the formation of cytotoxic xenoantibodies in rabbits. Serum HLA-A9 antigens were found by immunoprecipitation and gel electrophoresis to consist of a 45,000 m.w. heavy chain associated with beta2-microglobulin. The size of the HLA-lipid complex (less than 190,000 m.w.) and of the HLA-deoxycholate complex (less than 102,000 m.w.) suggests that HLA antigens are shed into plasma as a complex of a single HLA molecule and a single beta2-microglobulin chain, associated with boundary lipid.

subject areas

  • Antibodies
  • Blood
  • Chromatography, Gel
  • Cytotoxicity Tests, Immunologic
  • Electrophoresis, Polyacrylamide Gel
  • Fractional Precipitation
  • HLA Antigens
  • Histocompatibility Antigens
  • Humans
  • Immunosorbent Techniques
  • Lipoproteins, HDL
  • Ultracentrifugation
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Identity

International Standard Serial Number (ISSN)

  • 0022-1767

PubMed ID

  • 191523
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Additional Document Info

start page

  • 1004

end page

  • 1009

volume

  • 118

issue

  • 3

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