PRODUCTION OF HUMAN MATRIX METALLOPROTEINASE-3 (STROMELYSIN) IN ESCHERICHIA-COLI

被引：17

作者：

ROSENFELD, SA ^{[1
]}

ROSS, OH ^{[1
]}

CORMAN, JI ^{[1
]}

PRATTA, MA ^{[1
]}

BLESSINGTON, DL ^{[1
]}

FEESER, WS ^{[1
]}

FREIMARK, BD ^{[1
]}

机构：

[1] DUPONT MERCK PHARMACEUT CO, INFLAMMATORY DIS RES, WILMINGTON, DE 19880 USA

来源：

GENE | 1994年 / 139卷 / 02期

关键词：

RECOMBINANT DNA; INCLUSION BODIES; PROTEIN SOLUBILIZATION; PROTEIN REFOLDING; PURIFICATION; ENZYMATIC ACTIVITY;

D O I：

10.1016/0378-1119(94)90770-6

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Full-length human matrix metalloproteinase 3 (prostromelysin or proMMP-3) was produced in Escherichia coli as an intracellular insoluble aggregate that could be solublized and refolded to yield an activatable proenzyme. The refolded protein was purified to >95% homogeneity. The recombinant proMMP-3 (re-proMMP-3) could be activated by agents known to stimulate self-catalyzed cleavage of native fibroblast proMMP-3. The N-terminal amino-acid sequence of the re-proMMP-3 and its activation products indicated that they were the same as those obtained with the natural material.

引用

页码：281 / 286

页数：6

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