Comparison of human stromelysin and collagenase by cloning and sequence analysis.
Comparison of human stromelysin and collagenase by cloning and sequence analysis.
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通过克隆和序列分析比较人溶基质素和胶原酶。
DOI：
10.1042/bj2400913
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
A. Docherty
中科院分区：
文献类型：
--
作者：
S. Whitham;G. Murphy;P. Angel;H. Rahmsdorf;B. Smith;A. Lyons;T. Harris;J. Reynolds;P. Herrlich;A. Docherty
将人基质溶解素和胶原酶的dna来源氨基酸序列与纯化酶的n端序列进行比较，发现这些金属蛋白酶高度保守，并以前酶的形式分泌。通过与热溶酶的锌螯合序列的同源性，确定了一个假定的锌结合位点。这些序列允许鉴定：transin，一种在暴露于生长因子或被致癌病毒转化的大鼠成纤维细胞中诱导的蛋白质，作为基质溶解素的大鼠同源物；XHF1，一种在用致瘤剂治疗后在人成纤维细胞中诱导的蛋白质，作为胶原酶。
A comparison of the cDNA-derived amino acid sequences of human stromelysin and collagenase with the N-terminal sequences of purified enzymes reveals that these metalloproteinases are highly conserved and that they are secreted as proenzymes. A putative zinc-binding site was identified by its homology with the zinc-chelating sequence of thermolysin. These sequences permitted the identification of: transin, a protein induced in rat fibroblasts either exposed to growth factors or transformed by oncogenic viruses, as the rat homologue of stromelysin, and XHF1, a protein induced in human fibroblasts after treatment with tumourigenic agents, as collagenase.