Characterization of the ant ige nie epitope recognized by tumor selective antibody

I. M. Rose, D. L. Denardo, C. F. Meares

Research output: Contribution to journalArticlepeer-review


The selcriiviiy of Lym-1 for malignant li-jympliocytns makes this mono clonal antibody a promising randidaic for tho d('li\''i\ <>| toxit agents îo nia lignant It-cells. The original imrnunogen ued for the devflopmrnl of l.ym 1 was Raji Hnrkitt's lyniphoma cell nuclei [Kpstein AI,. Marder RJ. Winter -IX. Stathopouluh K. ('hen FM. Parker .IW. 'ray'or ('H I 17) Cancer Res -17:S:j()]. The Lym-1 antigen was characterised at that lime ,is a polymorphic HLA-DR variant. UV prepared an affinity column using immnhili/,ed I.yni-1 tn isolate t lie Lym-1 antigen from Raji cell lysate. Iiiniiunologi( al characierizalion of t he immnnoafïinity [mrified Lym-1 antigen on western blots led to the conclusion t hat the antigen i- thebeta chain of ULA-DRK). This was coitfinned by Ld man sequeiK'ine, oi the isolated polypeptide chain. V\estern blot.s fnrtiier stiuu that the Lym-1 epitope is only rerognued if the beta chain disnlfulr bonds are intact. These results imply that Lym 1 binds a discontinuous' epiîope on the beta chain of HLA-DR1Ü.

Original languageEnglish (US)
JournalFASEB Journal
Issue number9
StatePublished - 1997
Externally publishedYes

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology


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