Recombinant antibody-metallothionein: Design and evaluation for radioimmunoimaging

C. Das, P. V. Kulkarni, A. Constantinescu, P. Antich, F. R. Blattner, P. W. Tucker

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

We have produced a chimeric antibody (Ab) in which metallothionein, a well-characterized biological chelator of metals, was genetically fused to the F(ab′) domain of the S107 Ab heavy chain. Coexpression with the Ab light chain that conveys specificity for the synthetic antigen phosphocholine was achieved in plasmacytoma cells. Metal- and antigen-binding domains of the Ab-metallothionein hybrid function with normal avidity and specificity. Ab-metallothionein can be efficiently loaded with 99mTc and used to specifically bind phosphocholine-haptenated cells in vitro or to localize plasma-cell ascites tumors in mice. The approach offers potential advantages for producing radiolabeled Ab for targeted radiotherapy and diagnostic imaging.

Original languageEnglish (US)
Pages (from-to)9749-9753
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number20
Publication statusPublished - Oct 15 1992

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ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Das, C., Kulkarni, P. V., Constantinescu, A., Antich, P., Blattner, F. R., & Tucker, P. W. (1992). Recombinant antibody-metallothionein: Design and evaluation for radioimmunoimaging. Proceedings of the National Academy of Sciences of the United States of America, 89(20), 9749-9753.