Antibody-ricin conjugates: a method of linkage which blocks the galactose binding site of ricin.

B. M. Foxwell, W. C. Ross, P. E. Thorpe

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Conjugates of the monoclonal antibody anti-Thy 1:1 (OX7) and ricin have been constructed, using a thioether bond, such that the ricin no longer can bind Sepharose or asialofetuin. These conjugates were found to be very toxic to Thy 1:1 expressing AKR-A cells whereas they showed little toxicity to Thy 1:2 expressing EL4 cells. By comparison, OX7-ricin conjugates which retained galactose-binding capability were still highly toxic to EL4 cells and this toxicity was antagonized by lactose. A second conjugate made from the W3/25 monoclonal antibody was constructed. The W3/25-ricin conjugate which had lost Sepharose-binding capacity was toxic to W3/25 antigen-expressing rat T-leukaemia cells. This is in sharp contrast to the disulphide linked W3/25-ricin A-chain conjugate which is totally inactive, suggesting that the role of the B-chain in membrane transport of the A-chain into the cytosol is independent of galactose recognition.

Original languageEnglish (US)
Pages (from-to)101-107
Number of pages7
JournalBehring Institute Mitteilungen
Issue number74
StatePublished - May 1 1984

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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