通过克隆和序列分析对人基质溶素和胶原酶进行比较。
Comparison of human stromelysin and collagenase by cloning and sequence analysis.
作者信息
Whitham S E, Murphy G, Angel P, Rahmsdorf H J, Smith B J, Lyons A, Harris T J, Reynolds J J, Herrlich P, Docherty A J
出版信息
Biochem J. 1986 Dec 15;240(3):913-6. doi: 10.1042/bj2400913.
Abstract
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.
摘要
将人基质溶解素和胶原酶的互补DNA（cDNA）推导的氨基酸序列与纯化酶的N端序列进行比较，结果显示这些金属蛋白酶高度保守，且以酶原形式分泌。通过与嗜热菌蛋白酶的锌螯合序列同源性鉴定出一个假定的锌结合位点。这些序列使得能够鉴定出：转胶酶，一种在暴露于生长因子的大鼠成纤维细胞中诱导产生或由致癌病毒转化的蛋白质，作为基质溶解素的大鼠同源物；以及XHF1，一种在用致瘤剂处理后的人成纤维细胞中诱导产生的蛋白质，作为胶原酶。
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