@article{oai:mdu.repo.nii.ac.jp:00001014,
 author = {SHIBATA, YUKINAGA and FUJIMURA, SETSUO and NAKAMURA, TAKESHI},
 issue = {2},
 journal = {松本歯学},
 month = {Aug},
 note = {application/pdf, A peptidase hydrolyzing synthetic substrates of collagenase was purified from cell extract of an oral spirochete, Treponema denticola by sequential procedures including anionic ionexchange chromatography, gel filtration, and hydrophobic interaction chromatography. The purified enzyme was most active at pH 8.0 and was inhibited by p-chloromercuribenzoate or EDTA. This enzyme was active on Pz-peptide and Z-Gly-L-Pro-L-Leu-Gly-L-Pro. It was observed that Gly-L-Pro was released from the latter substrate, but proteins, including collagens, were not found to be hydrolyzed by this enzyme.},
 pages = {138--143},
 title = {Purification and Characterization of an Enzyme Produced by Treponema denticola Hydrolyzing Synthetic Collagenase Substrates},
 volume = {18},
 year = {1992}
}