Studies on the human lens have suggested that there is a differential regulation of the proteins in development. Work with a number of monoclonal antibodies indicates that maturation of human lens in terms of crystallin synthesis occurs at about the same time as the maturation of the retina. One of the low molecular weight proteins that begins to increase in content in the lens at about this time in development and become the major low molecular weight protein in the adult lens is absent in the cataractous zones of the lens. Immunological studies and high pressure liquid chromatography data have confirmed this decrease in microdissected lenses. The proteins of the primate lens have also been investigated using the Rhesus monkey lens. In addition to characterization of the proteins and mRNA in the lens, the glycoproteins have been studied using lectin binding. Glycoproteins with apparent molecular weights of 120,000, 90,000, 67,000 and 64,000 are closely associated with and may be intrinsic to the membrane of the lens. Similar glycoproteins have been seen in the human lens also.
