In a previous paper, we report a preliminary DSC study on bovine (BSA) and human (HSA) serum albumins. However, at accurate HPLC analysis the commercial proteins show three peaks: Fraction V-I, probably globulins (as declared by the producers), Fraction V-II (about 15-18% of the product) and Fraction V-III that represents pure BSA or HSA. A hypothesis is that the Fraction II is a covalent dimer, or trimer or a mixture of both, generated during the scalf-life of the commercial product. Denaturation enthalpies of the purified Fraction V-III and Fraction V-II of BSA, have been determined calorimetrically, at changing the pH, and the results of both compared with those obtained on the untreated protein. Few calorimetric experiments have been also carried on a BSA monomer derivative with sulphidril group protected. Computer program have been developed for the deconvolution of exo- and endothermic effects and for the analysis of thermal denaturation profiles.
Thermal denaturation of Bovine Serum Albumin and its oligomers and derivatives. II: pH dependence / G. Barone, S. Capasso, P. Del Vecchio, C. De Sena, D. Fessas, C. Giancola, G. Graziano, P. Tramonti. - In: JOURNAL OF THERMAL ANALYSIS. - ISSN 0368-4466. - 45:6(1995), pp. 1255-1264.
|Titolo:||Thermal denaturation of Bovine Serum Albumin and its oligomers and derivatives. II: pH dependence|
|Parole Chiave:||bovine serum albumin ; denaturation ; pH dependence|
|Settore Scientifico Disciplinare:||Settore CHIM/02 - Chimica Fisica|
|Data di pubblicazione:||1995|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1007/BF02547420|
|Appare nelle tipologie:||01 - Articolo su periodico|