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Fluorescence quenching studies of matrix metalloproteinases (MMPs): evidence for structural rearrangement of the proMMP-2/TIMP-2 complex upon mercurial activation.

Abstract:

Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases which are secreted from cells as zymogens and can be activated by treatment with organomercurial reagents or limited proteolysis. The proenzyme forms of MMP-2 (gelatinase A) and MMP-9 (gelatinase B) are found in complex with tissue inhibitor of metalloproteinases (designated proMMP-2/ TIMP-2 and proMMP-9/TIMP-1, respectively). The proposed mechanism of activation by mercurial compounds involves the induction of a conformationa...

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Publisher copy:
10.1006/abbi.1996.0377

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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Journal:
Archives of biochemistry and biophysics
Volume:
333
Issue:
1
Pages:
163-169
Publication date:
1996-09-05
DOI:
EISSN:
1096-0384
ISSN:
0003-9861
URN:
uuid:f154d9ab-b8aa-4bf5-ab26-1642a177cddd
Source identifiers:
411402
Local pid:
pubs:411402

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