Interaction of alpha-sarcin and gelonin with cibacron blue.
Alpha-sarcin and gelonin, two proteins which inactivate the 60S ribosomal subunit, interact with Cibacron blue and bind to blue dextran-Sepharose, from which they are partially desorbed by nucleoside triphosphates and, more efficiently, by homopolynucleotides. It is further shown that the two proteins bind to poly(U)-Sepharose and that homopolynucleotides protect dilute solutions of both inhibitors from inactivation. It is suggested that the presence of a polynucleotide site on alpha-sarcin is related to its ribonuclease activity. The existence of a similar site on gelonin might be a clue to its yet unknown mechanism of action.
D001667:Binding, Competitive; D003911:Dextrans; D004722:Endoribonucleases; D005656:Fungal Proteins / Q000378:metabolism* / Q000494:pharmacology; D009711:Nucleotides / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism* / Q000494:pharmacology; D011119:Polynucleotides / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects*; D014227:Triazines
D003911:Dextrans; D005656:Fungal Proteins; D009711:Nucleotides; D010940:Plant Proteins; D011119:Polynucleotides; D054789:Ribosome Inactivating Proteins, Type 1; D014227:Triazines; C014801:alpha-sarcin; C012842:Cibacron Blue F 3GA; C025674:GEL protein, Gelonium multiflorum; C017080:blue dextran; D004722:Endoribonucleases; D012260:Ribonucleases