INVESTIGADORES
PICO Guillermo Alfredo
artículos
Título:
Comparison between the thermodynamic features of a1-antitrypsin and human albumin partitioning in aqueous two-phase systems of polyethyleneglycol-dextran
Autor/es:
GUILLERMO ALFREDO PICO; NERLI, B; DINUCI, H.
Revista:
BIOPHYSICAL CHEMISTRY
Editorial:
Elsevier
Referencias:
Lugar: AMsterdand; Año: 2001 vol. 89 p. 219 - 229
ISSN:
0301-4622
Resumen:
The partitioning features of human serum albumin and 1-antitrypsin in aqueous two-phase systems of dextran
and polyethyleneglycol were studied. The effect of factors that affect the electrostatic term of Albertsson equation
such as pH, ionic strength, presence of neutral salts as well as those which affect the non-electrostatic term such as
polyethyleneglycol mol. wt. and temperature were assayed. At room temperature, the positive entropy and enthalpy
changes associated to the partition may be due to a release of part of the structured water in the domain of proteins
caused by H-bonds rupture when the proteins are transferred to the upper phase. This behaviour may be explained
on the basis of a preferential hydration of the proteins in presence of dextranbottom phase.and a preferential
interaction of polyethyleneglycols with the protein domaintop phase.. The electrostatic interactions were similar for
both proteins due to the proximity of their isoelectric point and similar dissociation profiles of their prototropic
groups.bottom phase.and a preferential
interaction of polyethyleneglycols with the protein domaintop phase.. The electrostatic interactions were similar for
both proteins due to the proximity of their isoelectric point and similar dissociation profiles of their prototropic
groups.top phase.. The electrostatic interactions were similar for
both proteins due to the proximity of their isoelectric point and similar dissociation profiles of their prototropic
groups.