ArticleBiotech (Basel (Switzerland))2023
Efficient Purification of Polyhistidine-Tagged Recombinant Proteins Using Functionalized Corundum Particles.
Article in Biotech (Basel (Switzerland)), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 2 citations in OpenAlex.
- Immobilized Metal Affinity Beads for Recombinant Protein Analysis by Desorption Electrospray Ionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2026Article
- A simple, rapid, resin-free platform for purification of vascular endothelial growth factor using a calcium-responsive fusion protein.Bioresources and bioprocessing · 2026Article
- Corundum Particles as Trypsin Carrier for Efficient Protein Digestion.Biotech (Basel (Switzerland)) · 2025Article
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immobilized metal affinity chromatography (IMAC) is a popular and valuable method for the affinity purification of polyhistidine-tagged recombinant proteins. However, it often shows practical limitations, which might require cumbersome optimizations, additional polishing, and enrichment steps. Here, we present functionalized corundum particles for the efficient, economical, and fast purification of recombinant proteins in a column-free format. The corundum surface is first derivatized with the amino silane APTES, then EDTA dianhydride, and subsequently loaded with nickel ions. The Kaiser test, well known in solid-phase peptide synthesis, was used to monitor amino silanization and the reaction with EDTA dianhydride. In addition, ICP-MS was performed to quantify the metal-binding capacity. His-tagged protein A/G (PAG), mixed with bovine serum albumin (BSA), was used as a test system. The PAG binding capacity was around 3 mg protein per gram of corundum or 2.4 mg per 1 mL of corundum suspension. Cytoplasm obtained from different
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