Works (1)
Updated: July 5th, 2023 15:59
2002 article
Purification and Characterization of the Fusion Protein Trypsin-Streptavidin Expressed in Escherichia coli
Zhao, F., Clare, D. A., Catignani, G. L., & Swaisgood, H. E. (2002, August 1). Journal of Protein Chemistry.
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
topics (OpenAlex): Biotin and Related Studies; Click Chemistry and Applications; Monoclonal and Polyclonal Antibodies Research
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.
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Added: August 6, 2018