Current Proteomics

Bernd Rehm  
Institute of Molecular BioSciences Massey University
Private Bag 11222
Palmerston North
New Zealand

Back

Spectral Methods of Characterizing the Conformational Changes of Glycated Goat Liver Cystatin

Author(s): Aaliya Shah, Mohd. Shahnawaz Khan, Medha Priyadarshini, Mohammad Aatif, Fakhra Amin, Bilqees Bano.

Abstract:

The interaction between proteins and sugars, termed as glycation has been a subject of increasing study over the past decade. The aim of the present study was to investigate the non-enzymatic interaction of thiol- proteinase inhibitor (cystatin) with three reducing sugars glucose, fructose and ribose. The behaviour of glycated cystatin was monitored by change in its hyperchromicity at 280nm, tryptophan fluorescence and Maillard fluorescence. The antipapain activity of glycated cystatin was found to be significantly lower than its non-glycated form. It was found that the incubation of cystatin with all the three sugars led to a parallel decrease in tryptophan fluorescence, enhancement in Maillard fluorescence and hyperchromicity in the UV-region. Among the three sugars studied ribose was found to be the most active in inducing structural and conformational alterations in the protein.

Keywords: Fructose, fluorescence, glycation, glucose, hyperchromicity, liver cystatin, maillard fluorescence, ribose, UV

Order Reprints Order Eprints Rights & PermissionsPrintExport

Article Details

VOLUME: 9
ISSUE: 4
Year: 2012
Page: [255 - 261]
Pages: 7
DOI: 10.2174/1570164611209040004
Price: $58