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Department of Animal Resource Production,3 the United Graduate School of Agricultural Science,
Departmentof Biology, Faculty of Education,4
Department of Biological Diversity and Resources,5 Faculty of Agriculture, Gifu University, Gifu 501-1193, Japan
Hokkaido National Fisheries Research Institute,6 Kushiro, Hokkaido 085-0802, Japan
Department of Zoology,7 College of Agriculture and Life Sciences, North Carolina State University, Raleigh, North Carolina 27695-7617
Graduate School of Fisheries Sciences,8 Hokkaido University, Hakodate, Hokkaido 041-8611, Japan
The objectives of this study were to characterize multiple forms of vitellogenin (Vg) in mosquitofish (Gambusia affinis) and to discover the fate of each Vg during its processing into product yolk proteins. Two Vg preparations, with apparent masses of 600 kDa (600 Vg) and 400 kDa (400 Vg), were isolated from the plasma of fish treated with estradiol-17ß (E2) by various chromatographic procedures. Immunological analyses verified the presence of two different Vg proteins (600 VgA and 600 VgB) in the 600 Vg preparation and of a single protein in the 400 Vg preparation. Three major yolk proteins (Yps) with apparent masses of 560, 400, and 28 kDa were observed in extracts of ovarian follicles from vitellogenic females. Immunological analyses demonstrated that the 400 Vg underwent no change in native mass after being incorporated into oocytes. The 600 Vgs gave rise to a 28 kDa ß'-component and a native 560 kDa Yp, which was heterodimeric in structure, consisting of two types of complexes between phosvitin (Pv) and lipovitellin (Lv) heavy- and light-chains. Full-length cDNAs encoding the 600 VgA, 600 VgB, and 400 Vg were isolated from a liver cDNA library of E2 treated fish. Similar to the zebrafish vg3 gene, the 400 Vg cDNA lacked a Pv domain and was classified as an incomplete or phosvitinless (C-type) Vg. The deduced primary structures of 600 VgA and 600 VgB were complete, and these were categorized as type A and type B Vgs, respectively, according to our recent classification scheme. This is the first report on the characterization of three functional Vg genes and their circulating and yolk protein products in any vertebrate species.
2 Correspondence: Sayumi Sawaguchi, Hokkaido National Fisheries Research Institute, 116, Katsurakoi, Kushiro, Hokkaido 085-0802 Japan. FAX: 81 154 91 9355; saysaw{at}fra.affrc.go.jp
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