Glycation of human γB-crystallin: A biophysical investigation

July 28, 2017

Title

Glycation of human γB-crystallin: A biophysical investigation

Author

Susmitnarayan Chaudhury, Pooja Ghosh, Sultana Parveen, Swagata Dasgupta

Year

2017

Journal

International Journal of Biological Macromolecules

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 28 days. 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.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Biochemistry