Chiou S H, Chang W P, Lai T A
Laboratory of Crystallin Research, National Taiwan University, Taipei.
Curr Eye Res. 1989 Oct;8(10):1055-61. doi: 10.3109/02713688908997398.
Characterization of lens crystallins from black swan, a rare aquatic bird belonging to the family Anatidae, was carried out to search for epsilon-crystallin with lactate dehydrogenase activity. Biochemical comparison of epsilon-crystallins isolated from the swan and duck lenses plus lactate dehydrogenase of chicken heart has also been made in order to establish the structural/functional relatedness of these proteins. Amino acid analyses showed essentially similar overall compositions for these three proteins. Kinetic analysis revealed differences between avian epsilon-crystallins and the authentic heart-type lactate dehydrogenase. The swan lenses similar to duck lenses appeared to contain a thermostable epsilon-crystallin which possesses very high enzymatic activity of lactate dehydrogenase. The characterization of epsilon-crystallins from the available species of aquatic birds may provide some insights into the evolution of this unique crystallin in the Aves and their enzymatic roles inside the lens.
对黑天鹅（一种属于鸭科的珍稀水鸟）晶状体中的晶状体蛋白进行了表征，以寻找具有乳酸脱氢酶活性的ε-晶状体蛋白。还对从天鹅和鸭晶状体中分离出的ε-晶状体蛋白与鸡心脏的乳酸脱氢酶进行了生化比较，以确定这些蛋白质的结构/功能相关性。氨基酸分析表明，这三种蛋白质的总体组成基本相似。动力学分析揭示了禽类ε-晶状体蛋白与正宗心脏型乳酸脱氢酶之间的差异。与鸭晶状体相似，天鹅晶状体似乎含有一种热稳定的ε-晶状体蛋白，它具有非常高的乳酸脱氢酶活性。对现有水鸟物种的ε-晶状体蛋白进行表征，可能有助于深入了解这种独特的晶状体蛋白在鸟类中的进化及其在晶状体中的酶促作用。
