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Thermodynamic Stability of Ribonuclease B
Authors:Del Vecchio  P  Catanzano  F  de Paola  B  Barone  G
Institution:(1) Department of Chemistry, University of Naples Federico II, Via Mezzocannone 4, 80134 Naples, Italy
Abstract:The thermodynamic stability of pancreatic ribonuclease B (RNase B), which possesses identical protein structure of pancreatic ribonuclease A (RNase A), but differs by the presence of a carbohydrate chain attached to Asn 34, was studied by means of differential scanning calorimetry (DSC) at different pH conditions. The comparison between the two proteins has shown a little but significant stabilization of RNase B with respect to the unglycosylated one at pH values higher than 7.0. The thermodynamic analysis reveals the carbohydrate moiety to have a small stabilization effect of 3 kJ mol–1 at pH 8.0 and 63°C on the protein. This revised version was published online in July 2006 with corrections to the Cover Date.
Keywords:DSC  glycosylated ribonuclease  thermodynamic stability
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