Abstract
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.
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