Abstract
N ɛ-(carboxymethyl)lysine, an advanced glycation end product, is present in the human lens. The effects of CML formation on protein conformation and stability were studied using the recombinant γC-crystallin as a model. Conformational change was studied by spectroscopic measurements such as fluorescence and circular dichroism. Conformational stability was determined by unfolding with heat. The results indicated that no conformational change was observed due to CML formation, but conformational stability decreased. These observations can be explained in terms of the relatively stable structure of γ-crystallin, especially when compared with other crystallins. The lens nucleus is rich in γ-crystallin and its stable conformation can assist γ-crystallin sustained insults and remain soluble.
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Liang, J.JN., Fu, L. Conformational Study of Nɛ-(carboxymethyl)lysine Adducts of Recombinant γC-crystallin. J Protein Chem 20, 641–645 (2001). https://doi.org/10.1023/A:1013768319488
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DOI: https://doi.org/10.1023/A:1013768319488