ArticleJournal of protein chemistry1999
Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein.
Article in Journal of protein chemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 43 citations in OpenAlex.
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- Plasmid Display for Stabilization of Enzymes Inside the Cell to Improve Whole-Cell Biotransformation Efficiency.Frontiers in bioengineering and biotechnology · 2019Article
- One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins.Microbial cell factories · 2018Article
- Fine Mutational Analysis of 2B8 and 3H7 Tag Epitopes with Corresponding Specific Monoclonal Antibodies.Molecules and cells · 2016Article
- Protein fusion tags for efficient expression and purification of recombinant proteins in the periplasmic space of E. coli.3 Biotech · 2016Review
- The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.Applied and environmental microbiology · 2008Article
- A simple vector system to improve performance and utilisation of recombinant antibodies.BMC biotechnology · 2006Article
- Effect of N-terminal solubility enhancing fusion proteins on yield of purified target protein.Journal of structural and functional genomics · 2006Article
- Bacterial expression strategies for human angiogenesis proteins.Journal of structural and functional genomics · 2006Article
- Characterization of the aggregates formed during recombinant protein expression in bacteria.BMC biochemistry · 2005Article
- Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.Cell stress & chaperones · 2005Article
- Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression.BMC biotechnology · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian aspartic proteinases procathepsin D and pepsinogen form insoluble inclusion bodies when expressed in bacteria. They become soluble but nonnative when synthesized as fusions to the carboxy terminus of E. coli maltose-binding protein (MBP). Since these nonnative states of the two aspartic proteinases showed no tendency to form insoluble aggregates, their biophysical properties were analyzed. The MBP portions were properly folded as shown by binding to amylose, but the aspartic proteinase moieties failed to bind pepstatin and lacked enzymatic activity, indicating that they were not correctly folded. When treated with proteinase K, only the MBP portion of the fusions was resistant to proteolysis. The fusion between MBP and cathepsin D had increased hydrophobic surface exposure compared to the two unfused partners, as determined by bis-ANS binding. Ultracentrifugal sedimentation analysis of MBP-procathepsin D and MBP-pepsinogen revealed species with very large and heterogeneous sedimentation values. Refolding of the fusions from 8 M urea generated proteins no larger than dimers. Refolded MBP-pepsinogen was proteolytically active, while only a few percent of renatured MBP-procathepsin D was obtained. The results suggest that MBP-aspartic proteinase fusions can provide a source of soluble but nonnative folding states of the mammalian polypeptides in the absence of aggregation.
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