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Journal of Lipid Research, Vol 26, 540-548, Copyright © 1985 by Lipid Research, Inc.
CR Duvic, G Smith, WE Sledge, LT Lee, MD Murray, PS Roheim, WR Gallaher and JJ Thompson
Heretofore, immunologic reagents used to define and quantify human Lp(a)
have been polyclonal in origin and therefore heterogeneous in antigenic
specificity. We report here the isolation of a mouse monoclonal antibody,
LHLP-1, monospecific for Lp(a). The antigen reactive with LHLP-1 was
expressed in both lipoprotein Lp(a) as well as apolipoprotein Lp(a)
delipidated by SDS treatment; however, disulfide reduction of
apolipoprotein Lp(a) inhibited LHLP-1 reactivity. The antigen reactive with
LHLP-1 on Lp(a), therefore, appears not to require lipid for expression of
its conformationally dependent (disulfide-inhibitable) epitope. Antigen
reactivity was virtually absent in the apoB and other proteins contained in
very low density, low density, and high density lipoprotein particles.
Immunologic quantification of Lp(a) in individual serum samples with a
rabbit reference antiserum or LHLP-1 showed good correlation. We conclude
that the monoclonal antibody LHLP-1 identifies an antigen unique to Lp(a)
and that this antibody may therefore be useful in the further
characterization and measurement of human Lp(a).
ARTICLES
Identification of a mouse monoclonal antibody, LHLP-1, specific for human Lp(a)
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