Purification and characterization of matrix metalloproteinase 9 from U937 monocytic leukaemia and HT1080 fibrosarcoma cells.

@article{Morodomi1992PurificationAC,
  title={Purification and characterization of matrix metalloproteinase 9 from U937 monocytic leukaemia and HT1080 fibrosarcoma cells.},
  author={T Morodomi and Yukie Ogata and Yasuyuki Sasaguri and Minoru Morimatsu and Hideaki Nagase},
  journal={The Biochemical journal},
  year={1992},
  volume={285 ( Pt 2)},
  pages={603-11}
}
The precursor of matrix metalloproteinase 9 (proMMP-9), also known as '92 kDa progelatinase/type IV procollagenase', was purified from the conditioned medium of U937 monocytic leukaemia and HT1080 fibrosarcoma cell lines stimulated with phorbol 12-myristate 13-acetate. ProMMP-9 in these culture media is non-covalently complexed with the 29 kDa tissue inhibitor of metalloproteinases (TIMP), but free proMMP-9 was separated from the TIMP-proMMP-9 complex by chromatography on Green A Dyematrex gel… CONTINUE READING
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