PRIMARY STRUCTURE OF BOVINE INTERSTITIAL COLLAGENASE DEDUCED FROM CDNA SEQUENCE

被引：8

作者：

TAMURA, M ^{[1
]}

SHIMOKAWA, H ^{[1
]}

SASAKI, S ^{[1
]}

机构：

[1] TOKYO MED & DENT UNIV,FAC DENT,DEPT BIOCHEM,BUNKYO KU,TOKYO 113,JAPAN

来源：

DNA SEQUENCE | 1994年 / 5卷 / 01期

关键词：

CDNA SEQUENCE; INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE; ZINC-BINDING DOMAIN;

D O I：

10.3109/10425179409039706

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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%.

引用

页码：63 / 66

页数：4

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