ISOLATION AND PARTIAL CHARACTERIZATION OF VITELLIN FROM THE EGG OF THE GIANT TIGER PRAWN, PENAEUS-MONODON

1. The results obtained from the present study show that vitellin (yol k protein), a glycolipoprotein derived from the giant tiger prawn, Pen aeus monodon, consists of four polypeptides, Ep1, Ep2, Ep3 and Ep4, wi th molecular weights of 168, 104, 83 and 74 kDa, respectively. This pr otein was purified using SDS-PAGE and gel-elution. 2. Antisera against Ep2, Ep3 and Ep4 fractions showed very strong specific binding reacti vity when reacted with shrimp ovaries at developing stages. 3. No cros sreaction was observed among Ep2, Ep3 and Ep4 fractions of vitellin. H owever, anti-Ep2 and anti-Ep3 were demonstrated to be able to react wi th Ep1 fraction. The homogenates obtained from ripe ovaries and hemoly mph of vitllogenesis females showed an immuno-identical pattern to tho se obtained from egg extracts. 4. The proteolysis mapping for each fra ction showed that Ep1, the high molecular weight fraction, contained E p2 and Ep3 fragments. These results suggest that Ep1 may be a precurso r for Ep2 and Ep3.