| Chapter title |
Expression and Purification of a Matrix Metalloprotease Transmembrane Domain in Escherichia coli
|
|---|---|
| Chapter number | 2 |
| Book title |
Matrix Metalloproteases
|
| Published in |
Methods in molecular biology, March 2017
|
| DOI | 10.1007/978-1-4939-6863-3_2 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-6861-9, 978-1-4939-6863-3
|
| Authors |
Charles A. Galea |
| Editors |
Charles A. Galea |
| Abstract |
Membrane tethered matrix metalloproteases are bound to the plasma membrane by a glycosylphosphatidylinositol-anchor or a transmembrane domain. To date, most studies of membrane-bound matrix metalloprotease have focused on the globular catalytic and protein-protein interaction domains of these enzymes. However, the transmembrane domains have been poorly studied even though they are known to mediate intracellular signaling via interaction with various cellular proteins. The expression and purification of the transmembrane domain of these proteins can be challenging due to their hydrophobic nature. In this chapter we describe the purification of a transmembrane domain for a membrane-bound matrix metalloprotease expressed in E. coli and its initial characterization by NMR spectroscopy. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 3 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 2 | 67% |
| Unknown | 1 | 33% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 1 | 33% |
| Unknown | 2 | 67% |