アメマスＳａｌｖｅｌｉｎｕｓ　ｌｅｕｃｏｍａｅｎｉｓビテロゲニンの卵黄蛋白質への特異的分解

DOI 日本農学文献記事索引 Web Site 被引用文献6件 参考文献14件
  • 平松 尚志
    北海道大学水産学部水産増殖学科淡水増殖学講座
  • 原 彰彦
    北海道大学水産学部附属七飯養魚実習施設

書誌事項

タイトル別名
  • Specific Proteolysis of Vitellogenin to Egg Yolk Proteins in White Spotted-charr Salvelinus leucomaenis.
  • アメマス Salvelinus leucomaenis ビテロゲニン ノ ラン

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抄録

Vitellogenin (Vg) was purified from white spotted-charr Salvelinus leucomaenis serum and biotinylated (b-Vg). The b-Vg was digested under mild acidic conditions by bovine cathepsin-D (BCD) or a water soluble fraction of charr eggs (WSF), Digests were analyzed by 5.0-22.5% gradient SDS-polyacrylamide gel electrophoresis (SDS-PAGE), Westem blotting, and gel filtration on Superose 6. Westem blotting was done using: 1) streptavidin coupled to horseradish peroxidase (HRPO) to identify biotinylated products of b-Vg digestion, and 2) antisera against lipovitellin (a-Lv) or β-component (a-β') to immunologically relate digestion products to specific charr egg yolk proteins. With respect to antigenicity and apparent molecular weight, fragments resulting from digestion of b-Vg by WSF or BCD were almost indistinguishable from those found in charr egg yolk, except for phosvitin (Pv). Pv-related phosphorus in BCD digests eluted at a position corresponding to a molecular weight slightly greater than that of Pv in egg yolk. The present study is the first to demonstrate in vitro conversion of salmonid Vg to its related egg yolk proteins. The similar catalytic effect of WSF or BCD on in vitro generation of egg yolk proteins suggests that cathepsin-D, present in WSF or intact eggs, may play a key role in natural yolk formation in salmonids.

収録刊行物

  • 日本水産学会誌

    日本水産学会誌 63 (5), 701-708, 1997

    公益社団法人 日本水産学会

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