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.
Thermodynamic stability of ribonuclease B / DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA; F., Catanzano; B., DE PAOLA; G., Barone. - In: JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY. - ISSN 1388-6150. - STAMPA. - 61:2(2000), pp. 363-368. [10.1023/A:1010101030232]
Thermodynamic stability of ribonuclease B.
DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA;
2000
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
