Purification and Characterization of Extracellular Matrix-degrading Metalloproteinase, Matrin (Pump-1), Secreted from Human Rectal Carcinoma Cell Line1

Abstract

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… (More)

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@inproceedings{Miyazaki1990PurificationAC, title={Purification and Characterization of Extracellular Matrix-degrading Metalloproteinase, Matrin (Pump-1), Secreted from Human Rectal Carcinoma Cell Line1}, author={Kaoru Miyazaki and Yasuhisa Hattori and Fuminori Umenishi and Hidetaro Yasumitsu and Makoto Umeda}, year={1990} }