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Abstract
Structural characteristics of glycoproteins, in general, and the correlation between certain compositional patterns of their glycans and the nature of the tissue elements with which they are associated are first discussed and demonstrated in a certain number of cases. On the other hand, it is pointed out that there appears to be a correlation between the ratio of the end groups of these glycans to each other and to the backbone constituent and functional properties of the glycoproteins. The preparation and analysis of glycoproteins of the lens of cattle and rabbits is then described, in three parts of the lens, namely, the equatorial, the polar, and the nuclear region. In rabbit lenses, these data were obtained in animals of different ages. It is shown that the concentration of glycoproteins in the equatorial region by far exceeds that in the polar and nuclear regions when calculated either by wet weight or in per cent of the albuminoid with which the glycoprotein fraction appears to be associated during centrifugation of lens homogenates at 6,000 and 10,000 x g. There were also significant differences between the three regions of lenses of adult rabbits as far as the ratio of neuraminic acid to fucose in the glycans of their glycoproteins is concerned.