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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).

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(...

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Publication status:
Published

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Publisher copy:
10.1021/bi026454l

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
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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

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