INVESTIGADORES
PICO Guillermo Alfredo
artículos
Título:
Thermodinamic study of the forces involved in the bovine serum albumin and ovalbumin partitioning in aqueos two phases systems
Autor/es:
GUILLERMO ALFREDO PICO; NERLI, B; ESPARIZ,
Revista:
BIOENGINEERING AND BIOTECHNOLOGY
Editorial:
John Wiley & Sons, Inc
Referencias:
Lugar: NY; Año: 2001 vol. 72 p. 448 - 474
ISSN:
0006-3592
Resumen:
The partitioning of bovine serum albumin and
ovalbumin in different two-phase aqueous polymer systems
is investigated using a thermodynamic approach.
Systems used were polyethylene glycols (PEGs) of molecular
weights 1000 to 10,000 Da and Dextran T500
(500,000 Da). Ovalbumin transfer to the top phase is exothermic,
which suggests an electrostatic interaction between
the hydroxyl groups of PEG and the hydrophilic
side chain of the protein, whereas the bovine serum albumin
partition is an endothermic process that is entropically
driven, which coincides with its high surface
hydrophobicity. The effect of PEG molecular weight on
enthalpy and heat capacity changes, associated with the
partition of both proteins, is examined on the basis of a
preferential interaction of low-molecular-weight PEG
with the protein surface.