Dipartimento di Scienze delle Produzioni Animali, Università degli Studi della Basilicata, Campus Universitario di Macchia Romana, 85100 Potenza, Italy.
Fish Shellfish Immunol. 2010 May-Jun;28(5-6):927-30. doi: 10.1016/j.fsi.2010.02.013. Epub 2010 Feb 17.
Blood and seminal plasma of brown trout Salmo trutta fario were analyzed for their iron binding potential adopting two different methods. Seminal plasma showed an iron binding capacity that was retained even if samples were exposed at acid pH, similarly to mammalian lactoferrin that binds ferric iron also at acid pH. This suggests that the iron binding capacity is determined by a factor having a lactoferrin-like activity. Moreover, trout seminal plasma proteins were also analyzed in their pattern by sodium dodecyl sulphate polyacrylamide gel elecrophoresis (SDS-PAGE) and electroblotted onto nitrocellulose membrane. When seminal plasma was subjected to immunoblotting using goat anti-bovine lactoferrin antibodies as a probe, only a single band having an apparent molecular weight of around 80 kDa was specifically detected, showing that this protein has homology with bovine lactoferrin.
采用两种不同方法分析了棕鳟鱼（Salmo trutta fario）的血液和精液血浆的铁结合能力。精液血浆显示出一种铁结合能力，即使在酸性 pH 值下暴露样品，也能保持这种能力，类似于在酸性 pH 值下结合三价铁的哺乳动物乳铁蛋白。这表明铁结合能力是由具有乳铁蛋白样活性的因子决定的。此外，还通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳 (SDS-PAGE) 分析了鳟鱼精液血浆蛋白的图谱，并将其电转移到硝酸纤维素膜上。当使用山羊抗牛乳铁蛋白抗体作为探针进行免疫印迹时，精液血浆中仅特异性地检测到一个具有约 80 kDa 表观分子量的单一条带，表明该蛋白与牛乳铁蛋白具有同源性。
