Williams J, Moreton K, D'Andrea G, Oratore A
Department of Biochemistry, University of Bristol, U.K.
Biochem Int. 1992 Oct;28(1):155-60.
Polymeric forms of hen ovotransferrin have been obtained by storage at 4 degrees C for 5 years or at 57 degrees C for 14 days and fractionated as dimers and tetramers by gel filtration on Sephadex. The ability of tyrosine to undergo nitration was reduced in the tetrameric protein, so that one could hypothesize that dityrosine formation is somewhat responsible of such polymerization process. Experimental data on the biological functionality showed that: i) dimeric ovotransferrin was able neither to bind nor to deliver iron; ii) tetrameric ovotransferrin was able to bind but not to deliver iron.
通过在4℃储存5年或在57℃储存14天获得了聚合形式的母鸡卵转铁蛋白，并通过在葡聚糖凝胶上进行凝胶过滤将其分离为二聚体和四聚体。四聚体蛋白中酪氨酸发生硝化的能力降低，因此可以推测二酪氨酸的形成在某种程度上促成了这种聚合过程。关于生物学功能的实验数据表明：i）二聚体卵转铁蛋白既不能结合也不能输送铁；ii）四聚体卵转铁蛋白能够结合但不能输送铁。
