동자개 Pseudobagrus fulvidraco의 난황단백질과 난황단백전구체의 분리와 면역학적 특성

Vitellogenin (Vg) is the precursor of vitellin (Vn), the major yolk protein of teleost fishes. In this study, Vg and Vn proteins of the Korean bullhead Pseudobagrus fulvidraco were isolated using gel-filtration chromatography (Sephadex-G 200 column) and anion-exchange chromatography (Mono Q HR 5/5 column), respectively. Purified Vn with an estimated molecular mass of 360 kDa by gel filtration chromatography was obtained from ovarian egg, and it was composited to one major subunit with an estimated molecular mass of 107 kDa by SDS-PAGE. In the result of western blotting, one major band was detected using antiserum against Vn (anti-Vn). These results suggested that Vn was composed of three subunits having the same molecular weight in Pseudobagrus fulvidraco. Vg was induced by estradiol-17β (E2) and purified from E₂ treated male serum. The molecular weight of whole Vg was estimated to be 450 kDa by gel filtration chromatography, and it is composed of three subunits with estimated molecular masses of 110 kDa, 125 kDa and 147 kDa as determined by SDS-PAGE. In the Ouchterlony’s immunodiffusion test using anti-Vn and antiserum against female and male serum, purified Vg was detected in matured female and E2 treated male serum but not in untreated male. These results can be used in detecting estrogenic contamination of the aquatic environment.