Thermodynamic Stability of Ribonuclease B |
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Authors: | Del Vecchio P Catanzano F de Paola B Barone G |
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Institution: | (1) Department of Chemistry, University of Naples Federico II, Via Mezzocannone 4, 80134 Naples, Italy |
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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. |
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Keywords: | DSC glycosylated ribonuclease thermodynamic stability |
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