Glycation of Ribonuclease A affects its enzymatic activity and DNA binding ability

Dinda, Amit Kumar ; Tripathy, Debi Ranjan ; Dasgupta, Swagata (2015) Glycation of Ribonuclease A affects its enzymatic activity and DNA binding ability Biochimie, 118 . pp. 162-172. ISSN 0300-9084

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Official URL: https://www.sciencedirect.com/science/article/pii/...

Related URL: http://dx.doi.org/10.1016/j.biochi.2015.09.014

Abstract

Prolonged non-enzymatic glycation of proteins results in the formation of advanced glycation end products (AGEs) that cause several diseases. The glycation of Ribonuclease A (RNase A) at pH 7.4 and 37 °C with ribose, glucose and fructose has been monitored by UV–vis, fluorescence, sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and matrix assisted laser desorption ionization spectroscopy-time of flight (MALDI-TOF) methods. The enzymatic activity and DNA binding ability of glycated RNase A was also investigated by an agarose gel-based assay. A precipitation assay examined the ribonucleolytic activity of the glycated enzyme. An increase in incubation time resulted in the formation of high molecular weight AGEs with a decrease in ribonucleolytic activity. Ribose exhibits the highest potency as a glycating agent and showed the greatest reduction in the ribonucleolytic activity of the enzyme. Interestingly, glycated RNase A was unable to bind with the ribonuclease inhibitor (RI) and DNA. The glycated form of the protein was also found to be ineffective in DNA melting unlike native RNase A.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Ribonuclease A; Advanced Glycation End Products (AGEs); AGE Cross-linking; Ribonucleolytic Activity; Ribonuclease Inhibitor; DNA Melting
ID Code:113388
Deposited On:10 May 2018 12:24
Last Modified:10 May 2018 12:24

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