Differential inhibition of protein synthesis in reticulocyte lysates and wheat germ extracts by a protein isolated from wheat germ extracts.
A protein with a molecular mass of 35-37 kDa has been isolated and partially purified from the postribosomal supernatant of wheat germ by ammonium sulfate precipitation (60-90%), Sephadex G-75, and DEAE-cellulose chromatography. It inhibited endogenous protein synthesis in rabbit reticulocyte lysates but had no effect on translation in wheat germ extracts. At low concentrations (0.34-1.36 ng/15 microliter assay), inhibition was limited to initiation of peptide synthesis. At higher concentrations (13.6 ng/15 microliter assay), elongation was also suppressed.
Wu
J M
JM
Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla.
D000818:Animals; D001798:Blood Proteins / Q000096:biosynthesis; D066298:In Vitro Techniques; D008970:Molecular Weight; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects; D010442:Peptide Chain Initiation, Translational / Q000187:drug effects; D010940:Plant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D014176:Protein Biosynthesis / Q000187:drug effects; D011500:Protein Synthesis Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D011817:Rabbits; D012156:Reticulocytes / Q000187:drug effects / Q000378:metabolism; D014908:Triticum
D001798:Blood Proteins; D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors