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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences >
Peer-reviewed Journal Articles, etc >
Purification of multiple vitellogenins in grey mullet (Mugil cephalus)
| Title: | Purification of multiple vitellogenins in grey mullet (Mugil cephalus) |
| Authors: | Amano, Haruna Browse this author | | Fujita, Toshiaki Browse this author | | Hiramatsu, Naoshi Browse this author | | Sawaguchi, Sayumi Browse this author | | Matsubara, Takahiro Browse this author | | Sullivan, Craig V Browse this author | | Hara, Akihiko Browse this author →KAKEN DB |
| Issue Date: | Nov-2007 |
| Publisher: | Springer |
| Journal Title: | Marine Biology |
| Volume: | 152 |
| Issue: | 6 |
| Start Page: | 1215 |
| End Page: | 1225 |
| Publisher DOI: | 10.1007/s00227-007-0768-z |
| Abstract: | Three female specific serum proteins were detected immunologically in the sera of grey mullet (Mugil cephalus) which were named vitellogenin A (VgA), VgB, and VgC, based upon their distinct antigenicity against specific antisera raised against three types of mullet lipovitellins (Lvs). These Vgs were subsequently purified from the serum of estradiol-treated mullet by combining several types of chromatography columns (anion exchanger, hydroxylapatite, immunoadsorbent column, and gel filtration). Purified native VgA, VgB, and VgC exhibited molecular masses of 570, 580, and 335 kDa, respectively. Following, SDS-PAGE, the estimated mass of polypeptide bands evident for VgA and VgB were ~179 kDa and ~175 kDa, respectively; VgC appeared to be ~132 kDa. The two larger Vgs (VgA and VgB) appeared to be phosphorylated, suggesting that these Vgs contain a highly phosphorylated, serine-rich phosvitin (Pv) domain. Furthermore, two discrete Vg-type specific antisera, anti-VgA and anti-VgB, were developed and each generated two precipitin lines against ovary extracts in immunoelectrophoresis, indicating that these Vgs contain additional antigenic yolk protein domains: Lv and β'-component. The small Vg (VgC) appeared to lack a Pv domain because of its low serine content (5.35%) and failure to show positive results in phospho-staining experiments. In conjunction with N-terminal amino acid sequencing analyses of the purified Vgs, our present results have conclusively identified the purified Vg products in grey mullet as typical A-type (VgA), B-type (VgB), and C-type (VgC) Vgs. |
| Rights: | The original publication is available at www.springerlink.com |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/30349 |
| Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 原 彰彦
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