AI Article Synopsis
- Glycation of ocular lens proteins is crucial in the development of diabetic cataracts, leading to impaired vision.
- An in vitro study was conducted on human γB-crystallin to measure glycation over 28 days in a high glucose solution.
- The study used various methods, including size exclusion chromatography and MALDI-TOF spectroscopy, to analyze the formation of advanced glycation end products and quantify glucose attachment.
Article Abstract
Glycation of ocular lens proteins plays a vital role in the development of diabetic cataract. In order to investigate the role of glycation in cataractogenesis, the extent of glycation of human γB-crystallin was determined by an in vitro glycation study in a solution of high glucose content for upto 28days. The glycated protein has been purified and the formation of advanced glycation end products (AGEs) has been monitored spectroscopically. Size exclusion chromatographic studies showed that the covalent intermolecular crosslinking in the dimer formed was not due to disulfide bond formation. MALDI-TOF spectroscopy was employed to determine the number of glucose moieties attached to the protein due to glycation.
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| http://dx.doi.org/10.1016/j.ijbiomac.2016.12.041 | DOI Listing |
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