2002 journal article

Purification and characterization of the fusion protein trypsin-streptavidin expressed in Escherichia coli


By: F. Zhao n, D. Clare n, G. Catignani n & H. Swaisgood n

author keywords: affinity column; fusion protein; protein expression; protein purification; trypsin; streptavidin
MeSH headings : Blotting, Western; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Escherichia coli / genetics; Recombinant Fusion Proteins / chemistry; Recombinant Fusion Proteins / genetics; Recombinant Fusion Proteins / isolation & purification; Streptavidin / chemistry; Trypsin / chemistry
TL;DR: The molecular size of the soluble purified fusion protein was determined by size-exclusion chromatography using Superose 12 FPLC, indicating that the soluble protein exists as a monomer; thus, the presence of the trypsin domain must prevent the streptavidin domain from tetramer formation. (via Semantic Scholar)
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