Characterization of a translation inhibitory protein from Luffa aegyptiaca

Sundaram Ramakrishnan, J. J. Enghlid, H. L. Bryant, F. J. Xu

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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 (US)
Pages (from-to)509-516
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume160
Issue number2
DOIs
StatePublished - Apr 28 1989
Externally publishedYes

Fingerprint

Luffa
Protein Biosynthesis
Proteins
Ricin
Transferrin Receptors
Ribosomal Proteins
Seeds
Molecular Weight
Monoclonal Antibodies
Seed
Molecular weight

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Characterization of a translation inhibitory protein from Luffa aegyptiaca. / Ramakrishnan, Sundaram; Enghlid, J. J.; Bryant, H. L.; Xu, F. J.

In: Biochemical and Biophysical Research Communications, Vol. 160, No. 2, 28.04.1989, p. 509-516.

Research output: Contribution to journalArticle

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