BACKGROUND: The relationship between structure (crystallin distribution) and function (refractive index) in the lens is not understood and can be studied by comparing biochemical and optical properties. Such a comparison has been made using a blue eyed trevally lens. METHODS: The optical parameter of refractive index distribution was determined using a nondestructive ray tracing technique. The distributions of the various classes of proteins in the lens were determined by dissolving lenses in concentric layers and using biochemical protein assay. HPLC and SDS-PAGE electrophoresis were used to investigate the proportion of proteins in each layer. RESULTS: The refractive index distribution, from center to edge, follows a second order polynomial. The proteins do not vary in their proportions over most of the lens; only in the inner-most regions is there a rapid increase in insoluble protein and a concomitant decrease in the soluble protein classes. The smallest proteins (gamma crystallins) become insoluble later than the alpha- and beta-crystallins. CONCLUSIONS: There are no similarities in the distributions of any of the protein classes to that of the refractive index in the fish lens. This result indicates that a quantitative relationship cannot be derived by comparing protein to refractive index distributions. However, the findings are consistent with those made in other species: a high content of gamma-crystallins is always found in lenses which have steep refractive index gradients and high index magnitudes.
BACKGROUND: The relationship between structure (crystallin distribution) and function (refractive index) in the lens is not understood and can be studied by comparing biochemical and optical properties. Such a comparison has been made using a blue eyed trevally lens. METHODS: The optical parameter of refractive index distribution was determined using a nondestructive ray tracing technique. The distributions of the various classes of proteins in the lens were determined by dissolving lenses in concentric layers and using biochemical protein assay. HPLC and SDS-PAGE electrophoresis were used to investigate the proportion of proteins in each layer. RESULTS: The refractive index distribution, from center to edge, follows a second order polynomial. The proteins do not vary in their proportions over most of the lens; only in the inner-most regions is there a rapid increase in insoluble protein and a concomitant decrease in the soluble protein classes. The smallest proteins (gamma crystallins) become insoluble later than the alpha- and beta-crystallins. CONCLUSIONS: There are no similarities in the distributions of any of the protein classes to that of the refractive index in the fish lens. This result indicates that a quantitative relationship cannot be derived by comparing protein to refractive index distributions. However, the findings are consistent with those made in other species: a high content of gamma-crystallins is always found in lenses which have steep refractive index gradients and high index magnitudes.
Authors: Arthur Laganowsky; Justin L P Benesch; Meytal Landau; Linlin Ding; Michael R Sawaya; Duilio Cascio; Qingling Huang; Carol V Robinson; Joseph Horwitz; David Eisenberg Journal: Protein Sci Date: 2010-05 Impact factor: 6.725