Lipovitellin（Lv）was purified from ovaries of mature female swordtai1 fish（Xiphophorus helleri）by gel filtration with Sephacryl S300 HR and anion exchange chromatography with HiTrap Q. The results indicated that the purified Lv appeared approximately 530 kD in native polyacrylamide gel electrophoresis(PAGE).Lv was characterized as a phospholipoglycoprotein by NativePAGE and staining of gels for carbohydrates, lipids and phosphorus. Polyclonal antibodies against the purified Lv from swordtai1 fish were produced in the mice. Double immunodiffusion showed that the determination of the titre for antiLv sera was l∶32. Westernblotting analyses demonstrated that antiLv sera have specificity and Lv has common antigenicity with vitellogenin(Vtg) while purified Vtg and Lv had crossreacted obviously with the antiLv sera. Double immunodiffusion showed that antiLv sera have sexspecificity and speciesspecificity.