Lens Protein

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Abstract
The vertebrate eye lens reveals two striking characteristics: transparency and an unusual high protein content. The major structural lens proteins are the so-called crystallins which contribute about 90% of the dry weight of the tissue. For about nine decades intensive studies have been devoted to the water-soluble crystallins. Only recently the water-insoluble proteins of the lens came also into the picture as a result of systematic investigations on the lenticular plasma membranes and the cytoskeleton. As far as the plasma membranes are concerned a 26,000 dalton polypeptide appeared to be the major constituent. This component which is characteristic for lens fiber membranes is also abundant in isolated lenticular junctions. It might well be that similar proteins occur in the gap junctions of other tissues. The lens is also a good source for the isolation of various enzymes. In particular leucine amino peptidase can easily be prepared from cattle lenses. The complete primary structure of this metallo-enzyme that consists of six identical subunits of molecular weight 54,000 has been solved recently in the author's laboratory. Since the lens is an organ that never sheds its cells lens tissue can also fruitfully be utilized for studies on postsynthetic changes of proteins and their modification and degradation upon aging.
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