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Characterization of a translation inhibitory protein from Luffa aegyptiaca

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  • S Ramakrishnan, Denmark
  • Jan J. Enghild
  • H L Bryant, Denmark
  • F J Xu, Denmark
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
A protein with a molecular weight of about 30,000 was purified from the seeds of Luffa aegyptiaca. This protein inhibited cell free translation at pM concentrations. In spite of functional similarity to other ribosomal inhibitory proteins, the NH2-terminal analysis did not show any significant homology. Competitive inhibition studies indicate no immunological crossreactivity between the inhibitory protein from Luffa aegyptiaca, pokeweed antiviral protein (PAP) and recombinant ricin A chain. Chemical linkage of the protein to a monoclonal antibody reactive to transferrin receptor resulted in a highly cytotoxic conjugate.
Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Volume160
Issue2
Pages (from-to)509-16
Number of pages7
ISSN0006-291X
Publication statusPublished - 1989

    Research areas

  • Amino Acid Sequence, Animals, Cross Reactions, Humans, Molecular Sequence Data, Molecular Weight, Plant Proteins, Protein Biosynthesis, Protein Synthesis Inhibitors, Rabbits, Ribosomes, Seeds, Sulfhydryl Compounds

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