- Abstract:
-
The inhibitory properties of TIMP-4 for matrix metalloproteinases (MMPs) were compared to those of TIMP-1 and TIMP-2. Full-length human TIMP-4 was expressed in E. coli, folded from inclusion bodies, and the active component was purified by MMP-1 affinity chromatography. Progress curve analysis of MMP inhibition by TIMP-4 indicated that association rate constants (k(on)) and inhibition constants (K(i)) were similar to those for other TIMPs ( approximately 10(5) M(-)(1) s(-)(1) and 10(-)(9)-10(...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi026454l
-
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- Journal:
- Biochemistry
- Volume:
- 41
- Issue:
- 50
- Pages:
- 15025-15035
- Publication date:
- 2002-12-05
- DOI:
- EISSN:
-
1520-4995
- ISSN:
-
0006-2960
- URN:
-
uuid:21a491df-fb22-4c1a-ac4b-51f628cfd407
- Source identifiers:
-
227136
- Local pid:
- pubs:227136
- Language:
- English
- Keywords:
- Copyright date:
- 2002
Journal article
E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A).
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