Ribonucleases constitute a ubiquitous superfamily of enzymes. Besides the well known hydrolytic activity against the RNAs, recently some of the proteins of this group, the so called RISBASE, have shown to possess a multiplicity of biological functions. In this article a short review is reported concerning systematic thermodynamic studies carried out at our laboratory mainly by means of differential scanning calorimetry on the well known ribonuclease A, RNase A, and its congeners. Among them, dimeric natural ribonuclease, BS-RNase, extracted from bull seminal plasma or vesicles, has shown very interesting features.
Thermodynamics of protein stability: a family of ribonucleases / Barone, G.; Catanzano, F.; DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA; Giancola, C.; Graziano, G.. - In: PURE AND APPLIED CHEMISTRY. - ISSN 0033-4545. - STAMPA. - 69:(1997), pp. 2307-2313.
Thermodynamics of protein stability: a family of ribonucleases.
DEL VECCHIO, POMPEA GIUSEPPINA GRAZIA;C. GIANCOLA;
1997
Abstract
Ribonucleases constitute a ubiquitous superfamily of enzymes. Besides the well known hydrolytic activity against the RNAs, recently some of the proteins of this group, the so called RISBASE, have shown to possess a multiplicity of biological functions. In this article a short review is reported concerning systematic thermodynamic studies carried out at our laboratory mainly by means of differential scanning calorimetry on the well known ribonuclease A, RNase A, and its congeners. Among them, dimeric natural ribonuclease, BS-RNase, extracted from bull seminal plasma or vesicles, has shown very interesting features.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
