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Purification of multiple vitellogenins in grey mullet (Mugil cephalus)

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/30349

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)

Submitter: 原 彰彦

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