A biochemical comparison has been made on the crystallins isolated from duck and frog lenses. Gel-permeation chromatography of lens homogenates from both classes on Fractogel TSK HW-55(S) revealed a homogeneous trimeric protein of 120 kDa in the duck lenses and a monomeric protein of 39 kDa in the frog lenses. Both crystallin fractions consist only of an approx. 38-kDa polypeptide in their subunit structures as determined by SDS gel electrophoresis. These two crystalline were compared with respect to their native molecular masses, subunit structures, peptide mapping and amino acid compositions in order to establish the identity of each crystallin. We have found differences in the protein structures of these two crystallins despite some degree of similarity in their amino acid compositions.
