Comparison between the thermodynamic features of α1-antitrypsin and human albumin partitioning in aqueous two-phase systems of polyethyleneglycol-dextran

Biophysical Chemistry

Volumn 89, Issue 2-3, 2001, Pages 219-229

  Di Nucci, Hernán ^a   Nerli, Bibiana ^a   Picó, Guillermo ^a  

^a UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

Author keywords

1 Antitrypsin; Albumin; Polyethyleneglycol; Two phase aqueous system

Indexed keywords

ALPHA 1 ANTITRYPSIN; DEXTRAN; HUMAN SERUM ALBUMIN; MACROGOL;

ARTICLE; ELECTRICITY; ENTROPY; HYDRATION; IONIC STRENGTH; PARTITION COEFFICIENT; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; THERMODYNAMICS;

ALPHA 1-ANTITRYPSIN; CHLORIDES; DEXTRANS; FLUORESCENT DYES; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MOLECULAR WEIGHT; OSMOLAR CONCENTRATION; POLYETHYLENE GLYCOLS; SERUM ALBUMIN; SOLVENTS; SURFACE PROPERTIES; TEMPERATURE; THERMODYNAMICS;

EID: 0035865710     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00237-4     Document Type: Article

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