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 language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Apr 28 1989|
Bibliographical noteFunding Information:
Antibodies to human receptor. As an and LRIP (1 ug/ml) viability (protein that the effect of using LRIP in the ACKNOWLEDGMENT : We wish to thank Ida B. Thogersen for technical assistance in protein sequencing. This work was supported by a grant from National Cancer Institute, CA 48068-01.