Use of chemically modified proteins to study the effect of a single protein property on partitioning in aqueous two-phase systems: Effect of surface hydrophobicity

Biotechnology and Bioengineering

Volumn 49, Issue 3, 1996, Pages 300-308

  Franco, T T ^a,c   Andrews, A T ^a   Asenjo, J A ^a,b  

^a UNIVERSITY OF READING   (United Kingdom)

^b UNIVERSITY OF CHILE   (Chile)

^c UNIVERSITY OF CAMPINAS   (Brazil)

Author keywords

hydrophobicity; partitioning in aqueous system; proteins, modified

Indexed keywords

ADDITION REACTIONS; BINARY MIXTURES; CHEMICAL MODIFICATION; CHROMATOGRAPHY; EFFECTS; MOLECULES; PHOSPHATES; POLYETHYLENE GLYCOLS; SODIUM CHLORIDE; SURFACE PROPERTIES;

AQUEOUS TWO PHASE SYSTEMS; BOVINE SERUM ALBUMIN; DEXTRAN; HYDROPHOBICITY; LACTOGLOBULIN; PARTITIONING;

PROTEINS;

AMINO ACID SUBSTITUTION; AQUEOUS SOLUTION; ARTICLE; CELL SPECIFICITY; CHEMICAL MODIFICATION; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PARTITION COEFFICIENT; PROTEIN ISOLATION; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; SURFACE PROPERTY;

BOVINAE;

EID: 0030569905     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960205)49:3<300::AID-BIT8>3.0.CO;2-O     Document Type: Article

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