Regular ArticleExpression of Human Placental Alkaline Phosphatase in Escherichia coli
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Development of recombinant secondary antibody mimics (rSAMs) for immunoassays through genetic fusion of monomeric alkaline phosphatase with antibody binders
2023, International Journal of Biological MacromoleculesA simple whole cell microbial biosensors to monitor soil pollution
2017, New Pesticides and Soil SensorsFunctional expression, purification, and characterization of the extra stable human placental alkaline phosphatase in the Pichia pastoris system
2004, Protein Expression and PurificationOverproduction of Bacterial Protein Disulfide Isomerase (DsbC) and Its Modulator (DsbD) Markedly Enhances Periplasmic Production of Human Nerve Growth Factor in Escherichia coli
2001, Journal of Biological ChemistryCitation Excerpt :Consistent with this proposal, expression of a bovine pancreatic trypsin inhibitor containing three disulfide bonds (nonconsecutive-type) yielded intermediates mostly with aberrant disulfide bonds in a dsbD deletion mutant (14). Similarly, the yield of active human placental alkaline phosphatase was low, whereas bacterial alkaline phosphatase was normally produced in thedipZ (dsbD) mutant presumably because of formation of aberrant disulfide bonds (39). It thus seems clear that DsbD, as well as DsbC, can become overloaded upon overexpression of heterologous proteins having multiple disulfide bonds.
Human placental alkaline phosphatase: Expression in Pichia pastoris, purification and characterization of the enzyme
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