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
收藏
页码：281 / 286
页数：6
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