VITELLINS AND VITELLOGENINS OF THE TERRESTRIAL ISOPOD, ARMADILLIDIUM VULGARE

¹ Laboratory of Biology, Kanagawa Prefectural College, Nakaocho 50-1, Asahiku, Yokohama 241, Japan

Four forms of vitellogenin (Vg·1-Vg·4) in the hemolymph and four forms of vitellin (Vn·1-Vn·4) in the oocytes of reproductive females of Armadillidium vulgare were detected by polyacrylamide gel electrophoresis (PAGE) at stage D of the molting cycle. All vitellogenins decreased and were not detected in the hemolymph at stage E. At stage E, Vn·1-Vn·3 disappeared; Vn·4 was the major vitellin component in mature oocytes. The electrophoretic patterns of vitellogenin and vitellin revealed changes correlated with the molting cycle and oocyte growth.

Vitellogenins were electrophoretically identical to vitellins. Rabbit anti-Vn·4 antibody cross-reacted with vitellogenins. Using Slater's method, the four forms of vitellin were glycolipoproteins, with molecular weights of Vn·1-700,000, Vn·2-620,000, Vn·3-540,000, and Vn·4-470,000. In SDS-PAGE, vitellin Vn·4 yielded three main polypeptide components with molecular weights of 80,000, 99,000, and 127,000. The polypeptide compositions among vitellins (Vn·1-Vn·4) were similar.