金属蛋白酶组织抑制剂-2（TIMP-2）功能域的表征

DeClerck Y A, Yean T D, Lee Y, Tomich J M, Langley K E

Division of Hematology/Oncology, Childrens Hospital, Los Angeles, CA 90027.

Biochem J. 1993 Jan 1;289 ( Pt 1)(Pt 1):65-9. doi: 10.1042/bj2890065.

Analysis of the functional domain of tissue inhibitor of metallo-proteinases-2 (TIMP-2) was performed using limited proteolytic degradation with trypsin. This treatment generated a 13.5 kDa fragment which was purified and shown to consist of an uncleaved N-terminal region extending from residue 1 to residue 132. The fragment retains the ability to inhibit activated interstitial collagenase and to block the autocatalytic activation of procollagenase.

利用胰蛋白酶进行有限的蛋白水解降解，对金属蛋白酶组织抑制剂-2（TIMP-2）的功能域进行了分析。这种处理产生了一个13.5 kDa的片段，该片段经过纯化后显示由从第1位残基延伸至第132位残基的未切割N端区域组成。该片段保留了抑制活化的间质胶原酶和阻断前胶原酶自催化激活的能力。