| First Author | Lemaître V | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 230 |
| Issue | 1 | Pages | 202-5 |
| PubMed ID | 9020046 | Mgi Jnum | J:37563 |
| Mgi Id | MGI:84954 | Doi | 10.1006/bbrc.1996.5924 |
| Citation | Lemaitre V, et al. (1997) The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides. Biochem Biophys Res Commun 230(1):202-5 |
| abstractText | The sequence coding for the catalytic domain of mouse collagenase-3 (MMP-13) was amplified by polymerase chain reaction and expressed in Escherichia coli. The recombinant catalytic domain (CCD), mainly recovered as inclusion bodies, was renatured and purified to homogeneity by preparative SDS-PAGE. The purified CCD degraded gelatin, casein and a synthetic peptide. CCD was not able to cleave the triple-helical domain of type I collagen but conserved the specific property of full-length collagenase-3 to cleave the N-telopeptides. These results show that residues involved in the recognition and cleavage of the aminotelopeptides of type I collagen are located in the catalytic domain of mouse collagenase-3 and that the C-terminal domain is not required for this activity. |
