Purification and properties of the low-molecular-weight alpha-crystallin from normal goat lens: comparison with bovine lens.

Low-molecular-weight alpha-crystallin (alpha L-crystallin) isolated from decapsulated lens of goat (Capra hiscus) has been purified to an apparently homogeneous population. Goat alpha L-crystallin closely resembles its bovine counterpart in size, shape, exposition of sulfhydryl groups, subunit composition and the nature of its UV-absorption profile. Like bovine alpha L-crystallin, dissociated subunits of goat alpha L-crystallin assemble upon reassociation into a particle of almost half the size of the native one. However, subunits of goat alpha L-crystallin are found to contain more aromatic amino acid residues than those of bovine subunits leading to a higher value of extinction coefficient (E1cm1%) at 280 nm for the goat protein.