Abstract
Low-molecular-weight α-crystallin ( α L-crystallin) isolated from decapsulated lens of goat ( Capra hiscus) has been purified to an apparently homogeneous population. Goat α 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 α L-crystallin, dissociated subunits of goat α L-crystallin assemble upon reassociation into a particle of almost half the size of the native one. However, subunits of goat α L-crystallin are found to contain more aromatic amino acid residues than those of bovine subunits leading to a higher value of extinction coefficient ( E 1 cm 1%) at 280 nm for the goat protein.
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