Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line.

@article{Miyazaki1990PurificationAC,
  title={Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line.},
  author={Kaoru Miyazaki and Yutaka Hattori and Fuminori Umenishi and Hidetaro Yasumitsu and Makoto Umeda},
  journal={Cancer research},
  year={1990},
  volume={50 24},
  pages={7758-64}
}
A metalloproteinase with Mr 29,000 was purified to homogeneity as a latent proenzyme from the conditioned medium of a human rectal carcinoma cell line CaR-1. This enzyme hydrolyzed casein more potently than gelatin embedded in polyacrylamide gels in zymography assay. Calcium ion was essential for the activity. It exerted the maximum activity at pH 7-9. Its activity was stimulated by organomercurials, such as p-amino-phenyl mercuric acetate and p-chloromercuric benzoic acid, and was inhibited by… CONTINUE READING
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