Primary structure of bovine interstitial collagenase deduced from cDNA sequence
1994
Interstitial collagenase (EC 3.4.24.7, MMP-1) is a member of a family of metalloproteinases and is thought to play a role in extracellular matrix remodeling. We have isolated and sequenced a cDNA for bovine interstitial collagenase from a periodontium fibroblast cDNA library. An insert of the cDNA we isolated was 2,025 bp containing an open reading frame which encodes a sequence of 469 amino acids. The identity at the amino acid level between bovine and human interstitial collagenase was 88%, between bovine and rabbit 85% and between bovine and porcine 87%. However, sequence similarity of mouse and rat interstitial collagenases to that of bovine was revealed 55%.
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