Faucher D, Lelièvre Y, Boiziau J, Cornet P, Cartwright T
Rhône-Poulenc Santé (CRMA), Site de Recherche de Monts, France.
Pathol Biol (Paris). 1989 Mar;37(3):199-205.
A potent collagenase inhibitor was purified from cells of calf aorta medial tissue maintained in culture. This molecule was characterized and identified as TIMP (Tissue Inhibitor of Metalloproteinases). Formation of a TIMP--collagenase complex was demonstrated chromatographically using pure TIMP and pure pig synovial cell collagenase. The N-terminal aminoacid sequence of TIMP was determined and, using appropriate oligonucleotide probes the human genes was cloned from a human cDNA bank. This gene was expressed in E. coli, and fully active TIMP was obtained after a denaturation renaturation process. The interest of TIMP as a model for the design of novel collagenase inhibitors is discussed.
从培养的小牛主动脉中层组织细胞中纯化出一种强效胶原酶抑制剂。该分子经鉴定为金属蛋白酶组织抑制剂（TIMP）。使用纯TIMP和纯猪滑膜细胞胶原酶通过色谱法证明了TIMP - 胶原酶复合物的形成。测定了TIMP的N端氨基酸序列，并使用合适的寡核苷酸探针从人cDNA文库中克隆了人类基因。该基因在大肠杆菌中表达，并经过变性复性过程后获得了完全活性的TIMP。讨论了TIMP作为新型胶原酶抑制剂设计模型的意义。
