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Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate.

Abstract:

Tissue inhibitor of metalloproteinases (TIMP)-2 forms a noncovalent complex with the precursor of matrix metalloproteinase 2 (proMMP-2, progelatinase A) through interaction of the C-terminal domain of each molecule. We have isolated the proMMP-2-TIMP-2 complex from the medium of human uterine cervical fibroblasts and investigated the processes involved in its activation by 4-aminophenylmercuric acetate (APMA). The treatment of the complex with APMA-activated proMMP-2 by disrupting the Cys73-Z...

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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Journal:
The Biochemical journal
Volume:
308 ( Pt 2)
Pages:
645-651
Publication date:
1995-06-05
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:0511450c-487e-4c52-b585-4b934cc551d6
Source identifiers:
411409
Local pid:
pubs:411409

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