PURIFICATION AND CHARACTERIZATION OF APLYSIANIN-E, AN ANTITUMOR FACTOR FROM SEA HARE EGGS

  • 1 November 1987
    • journal article
    • research article
    • Vol. 47  (21) , 5649-5653
Abstract
An antitumor factor, aplysianin E, inducing tumor lysis was purified to apparent homogeneity from the supernatant of a homogenate of eggs of the sea hare Aplysia kurodai. Purified aplysianin E was a 250-kDa glycoprotein containing three different-subunits. This factor was half-maximally active at 2-114 ng protein/ml and lysed all the tumor cells tested but did not lyse normal white or red blood cells. Aplysianin E was labile on treatments with heat, low pH, urea, guanidine, sodium lauryl sulfate, and periodate, but not with proteases or organic solvents. Aplysianin E completely inhibited the syntheses of DNA, RNA, and protein by tumor cells within 2 h and caused their complete cytolysis within 15 h. Tumor lysis by aplysianin E was inhibited by N-acetylneuraminic acid, suggesting that recognition of the sugar moiety is a key step in cytolysis induced by aplysianin E. Aplysianin E also prolonged the survival of mice bearing syngeneic MM46 ascites or solid tumors. These results suggest that aplysianin E, found in an invertebrate, the sea hare, is a new antitumor factor.