High-fidelity translation of recombinant human hemoglobin in Escherichia coli

Article Abstract:

Recombinant human hemoglobin was expressed in the heterologous expression system of Escherichia coli. Di-alpha-globin and beta-globin genes were coexpressed and formed soluble, functional recombinant human hemoglobin upon the addition of heme. The absent amino acid analysis method was used to examine the fidelity of heterologous translation in E. coli. Results reveal that the translation has an error rate of at most 0.0001, typical of translation error rates for E. coli proteins.

Evaluation, Genetic translation, Translation (Genetics)

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Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli

Article Abstract:

A physical model integrating hemoglobin synthesis, folding and heme association in recombinant Escherichia coli is presented. According to the model, low temperature stabilizes the apoglobin. Globin synthesis in E. coli does not allow complete folding prior to the release of the polypeptide from the ribosomes. The apoglobin then is trapped in a semifolded configuration largely affected by temperature changes in the absence of heme.

Physiological aspects

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A mutation that improves soluble recombinant hemoglobin accumulation in Escherichia coli in heme excess

Article Abstract:

Research was conducted to examine the effects of heme concentration and mutations on soluble rHb accumulation. Results suggest that high-level accumulation of soluble rHb necessitates the use of excess heme and depends on the amino acid sequence of the globin protein. The most important improvements in soluble expression were observed with rHbs containing amino acid substitutions in beta-globin.

Gene mutations, Gene mutation, Recombinant proteins, Heme

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