Purification and Characterization of Extracellular Matrix-degrading Metalloproteinase , Matrin ( Pump-1 ) , Secreted from Human Rectal Carcinoma Cell Line 1

@inproceedings{Miyazaki2006PurificationAC,
  title={Purification and Characterization of Extracellular Matrix-degrading Metalloproteinase , Matrin ( Pump-1 ) , Secreted from Human Rectal Carcinoma Cell Line 1},
  author={Kaoru Miyazaki and Yasuhisa Hattori and Fuminori Umenishi and Hidetaro Yasumitsu and Makoto Umeda},
  year={2006}
}
A metalloproteinase with M, 29,000 was purified to homogeneity as a latent proenzyme from the conditioned medium of a human rectal carci noma 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-aminophenyl mercuric acetate and p-chloromercuric benzoic acid, and was inhibited by… CONTINUE READING