Characterization of a translation inhibitory protein from Luffa aegyptiaca.
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.
Ramakrishnan
S
S
Department of Medicine, Duke University Medical Center, Durham, NC 27710.
Enghlid
J J
JJ
Bryant
H L
HL
Xu
F J
FJ
D000595:Amino Acid Sequence; D000818:Animals; D003429:Cross Reactions; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000633:toxicity; D014176:Protein Biosynthesis / Q000187:drug effects*; D011500:Protein Synthesis Inhibitors / Q000276:immunology / Q000302:isolation & purification* / Q000633:toxicity; D011817:Rabbits; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D012639:Seeds / Q000032:analysis; D013438:Sulfhydryl Compounds
D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D013438:Sulfhydryl Compounds