@article{oai:mdu.repo.nii.ac.jp:00000918,
 author = {SHIBATA, YUKINAGA and HOSHINO, TERUMUNE and FUJIMURA, SETSUO and NAKAMURA, TAKESHI},
 issue = {2},
 journal = {松本歯学},
 month = {Aug},
 note = {application/pdf, Gelatinase in the culture supernatant of Prevotella intermedia was purified to homogeneity by the combined procedure of ethanol precipitation and three steps of chromatography. The enzyme was a cystein protease with a molecular mass of 45 kDa. The activity was inhibited by divalent metal chelators and its inhibition was recovered by the addition of Ca^<2+>. The optimum pH for activity was 7.0-7.5 and the enzyme was inactivated by heating at 60℃ for 10 min. It hydrolyzed actively azocoll and hide powder besides gelatin. Hydrolysis of type IV collagen, if not strong, was also observed.},
 pages = {180--184},
 title = {Isolation and Properties of an Extracellular Gelatinase from a Strain of Prevotella intermedia Which Coelaborates Elastase},
 volume = {20},
 year = {1994}
}