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Abstract
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 (600Vg) and
400 kDa (400Vg), were isolated from plasma of
estradiol-17
(E2) treated fish by
various chromatographic procedures. Immunological
analyses verified the presence of two different Vg
proteins (600VgA and 600VgB) in the 600Vg preparation and
of a single protein in the 400Vg 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 400Vg underwent no change in native mass after
being incorporated into oocytes. The 600Vgs gave rise to
a 28 kDa '-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
600VgA, 600VgB, and 400Vg were isolated from a liver cDNA
library of E2 treated fish. Similar to the
zebrafish vg3 gene, the 400Vg cDNA lacked a Pv
domain and
was classified as an incomplete or phosvitinless (C-type)
Vg. The deduced primary structures of the 600VgA and
600VgB 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
characterization of three functional Vg genes and their
circulating and yolk protein products in any vertebrate
species.
Key words:
Gamete Biology •
Ovary •
Estradiol •
Gametogenesis •
Oocyte development
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