THE COLLAGEN-BINDING SITE OF TYPE-II UNITS OF BOVINE SEMINAL FLUID PROTEIN PDC-109 AND FIBRONECTIN
THE COLLAGEN-BINDING SITE OF TYPE-II UNITS OF BOVINE SEMINAL FLUID PROTEIN PDC-109 AND FIBRONECTIN
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DOI：
10.1111/j.1432-1033.1990.tb19403.x
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发表时间：
1990-11-13
期刊：
影响因子：
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通讯作者：
PATTHY, L
中科院分区：
文献类型：
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作者：
BANYAI, L;TREXLER, M;PATTHY, L
通过对结合胶原蛋白的牛精液蛋白PDC - 109进行有限的蛋白水解，分离出单一的II型结构域。与亲本分子的第二类结构域相对应的45 -残基片段被发现对固定的胶原具有亲和力，这表明该小结构域携带胶原结合位点的关键区域。对纤维连接蛋白的各种片段的研究也暗示了该分子的两种II型单位在胶原蛋白结合中。在目前的工作中，我们发现大肠杆菌β -半乳糖苷酶融合蛋白表达的人纤维连接蛋白的II型结构域特异性地与固定的胶原结合。
A single type‐II domain has been isolated by limited proteolysis of the collagen‐binding bovine seminal fluid protein, PDC‐109. The 45‐residue fragment corresponding to the second type‐II domain of the parent molecule was found to have retained affinity for immobilized collagen, indicating that this minidomain carries critical regions of the collagen‐binding site. Studies on various fragments of fibronectin have also implicated the two type‐II units of this molecule in collagen‐binding. In the present work we have found that type‐II domains of human fibronectin, expressed inEscherichia colias β‐galactosidase fusion proteins, bind specifically to immobilized collagen.