Abstract
WITH ageing, a number of significant changes occur in the chemistry of the human lens. In the central region of the organ there is a slow transformation of protein to high molecular weight (HMW) aggregates greater than 50 × 106 (refs 1 and 2). It has been suggested that the relatively high concentration of such protein species in older lenses may cause significant light scattering3,4 and may be a contributing factor in the development of senile cataract characterised by central sclerosis and opacification1. An age-dependent increase in the insoluble protein fraction has also been observed5–8 and recent experiments indicate that the HMW species is an intermediate in the formation of this material15. Marked changes in the polypeptide chains of human lens proteins probably largely attributable to post-translational transformation, have also been observed16.
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References
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DILLON, J., SPECTOR, A. & NAKANISHI, K. Identification of β carbolines isolated from fluorescent human lens proteins. Nature 259, 422–423 (1976). https://doi.org/10.1038/259422a0
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DOI: https://doi.org/10.1038/259422a0
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