Kato Y, Ogawa K, Yamamoto S, Abe S, Kishi J, Hayakawa T
Bio-Science Laboratory, Asahi Chemical Industry Co. Ltd., Shizuoka, Japan.
FEBS Lett. 1990 Jul 30;268(1):39-42. doi: 10.1016/0014-5793(90)80967-n.
A novel type IV collagen-degrading metalloproteinase was purified from the conditioned media of a murine metastatic sarcoma cell line. The molecular weight of the purified enzyme was determined to be 100 kDa by SDS-PAGE, while 700 kDa by gel filtration suggesting that the enzyme has a multimer structure. This enzyme degrades type IV collagen, but neither type I collagen nor casein. The failure of trypsin treatment to enhance the enzyme activity suggested that the purified enzyme did not require activation. Although the enzyme seems to be classified as a matrix metalloproteinase, it was inhibited by neither tissue inhibitor of metalloproteinases (TIMP) nor TIMP-2 and thus represents a novel type IV collagen-degrading metalloproteinase.
从鼠转移性肉瘤细胞系的条件培养基中纯化出一种新型的IV型胶原降解金属蛋白酶。通过SDS-PAGE测定，纯化酶的分子量为100 kDa，而通过凝胶过滤测定为700 kDa，这表明该酶具有多聚体结构。这种酶可降解IV型胶原，但不降解I型胶原和酪蛋白。胰蛋白酶处理不能增强该酶的活性，这表明纯化的酶不需要激活。尽管该酶似乎可归类为基质金属蛋白酶，但它既不受金属蛋白酶组织抑制剂（TIMP）也不受TIMP-2的抑制，因此代表一种新型的IV型胶原降解金属蛋白酶。
