| Title |
Expression and Purification of Recombinant Hemoglobin in Escherichia coli
|
|---|---|
| Published in |
PLOS ONE, May 2011
|
| DOI | 10.1371/journal.pone.0020176 |
| Pubmed ID | |
| Authors |
Chandrasekhar Natarajan, Xiaoben Jiang, Angela Fago, Roy E. Weber, Hideaki Moriyama, Jay F. Storz |
| Abstract |
Recombinant DNA technologies have played a pivotal role in the elucidation of structure-function relationships in hemoglobin (Hb) and other globin proteins. Here we describe the development of a plasmid expression system to synthesize recombinant Hbs in Escherichia coli, and we describe a protocol for expressing Hbs with low intrinsic solubilities. Since the α- and β-chain Hbs of different species span a broad range of solubilities, experimental protocols that have been optimized for expressing recombinant human HbA may often prove unsuitable for the recombinant expression of wildtype and mutant Hbs of other species. |
Mendeley readers
The data shown below were compiled from readership statistics for 78 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United Kingdom | 3 | 4% |
| United States | 2 | 3% |
| Indonesia | 1 | 1% |
| Unknown | 72 | 92% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 14 | 18% |
| Researcher | 11 | 14% |
| Student > Bachelor | 11 | 14% |
| Student > Postgraduate | 6 | 8% |
| Student > Master | 5 | 6% |
| Other | 14 | 18% |
| Unknown | 17 | 22% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 23 | 29% |
| Biochemistry, Genetics and Molecular Biology | 21 | 27% |
| Chemistry | 5 | 6% |
| Engineering | 4 | 5% |
| Immunology and Microbiology | 2 | 3% |
| Other | 4 | 5% |
| Unknown | 19 | 24% |