| Chapter title |
Purification of Proteins Fused to Maltose-Binding Protein.
|
|---|---|
| Chapter number | 13 |
| Book title |
Protein Chromatography
|
| Published in |
Methods in molecular biology, January 2017
|
| DOI | 10.1007/978-1-4939-6412-3_13 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6410-9, 978-1-4939-6412-3
|
| Authors |
Mario Lebendiker Ph.D., Tsafi Danieli, Mario Lebendiker, Lebendiker, Mario, Danieli, Tsafi |
| Editors |
Dermot Walls, Sinéad T. Loughran |
| Abstract |
Maltose-Binding Protein (MBP) is one of the most popular fusion partners being used for producing recombinant proteins in bacterial cells. MBP allows the use of a simple capture affinity step on Amylose-Agarose or Dextrin-Sepharose columns, resulting in a protein that is often 70-90 % pure in a single step. In addition to protein isolation applications, MBP provides a high degree of translation, and facilitates the proper folding and solubility of the target protein. This paper describes efficient procedures for isolating highly purified MBP target proteins. Special attention is given to considerations for downstream applications such as structural determination studies, protein activity assays, and assessing the chemical characteristics of the target protein. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United Kingdom | 1 | <1% |
| Unknown | 116 | 99% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Bachelor | 24 | 21% |
| Student > Master | 16 | 14% |
| Researcher | 14 | 12% |
| Student > Ph. D. Student | 13 | 11% |
| Student > Doctoral Student | 5 | 4% |
| Other | 13 | 11% |
| Unknown | 32 | 27% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 40 | 34% |
| Agricultural and Biological Sciences | 25 | 21% |
| Chemistry | 6 | 5% |
| Engineering | 3 | 3% |
| Pharmacology, Toxicology and Pharmaceutical Science | 2 | 2% |
| Other | 6 | 5% |
| Unknown | 35 | 30% |