Improved partitioning in aqueous two-phase system of tyrosine-tagged recombinant lactate dehydrogenase.

doi:10.1016/s1046-5928(02)00008-6

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Article

Improved partitioning in aqueous two-phase system of tyrosine-tagged recombinant lactate dehydrogenase.

Protein expression and purification - 1 Jul 2002

Fexby Sara, Bülow Leif

Abstract excerpt

The partitioning of Bacillus stearothermophilus lactate dehydrogenase (LDH) in an aqueous two-phase system was studied. Particularly, the influence of tyrosine tags on the partitioning was evaluated. The hydrophobic effect, caused by the addition of tyrosine residues, was determined in a system based on dextran and the thermoseparating ethylene oxide-propylene oxide random copolymer (EO30PO70). Five different LDH...

Topics

Amino Acid Sequence
Enzyme Stability
Geobacillus stearothermophilus
L-Lactate Dehydrogenase
Models, Molecular
Molecular Sequence Data
Mutation
Polyethylenes
Polypropylenes
Protein Conformation
Recombinant Fusion Proteins
Solutions
Tyrosine
Water

Source

Open in PubMed

Identifiers

PMID: 12135559
DOI: 10.1016/s1046-5928(02)00008-6

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