@article{oai:mdu.repo.nii.ac.jp:00001199,
 author = {吉村, 隆二 and 柴田, 幸永 and 藤村, 節夫 and 中村, 武},
 issue = {2},
 journal = {松本歯学},
 month = {Aug},
 note = {application/pdf, Screening tests of gingival crevice dental plaque conducted to detect the bacterial strains responsible for degradation of acid-mucopolysaccharides provided an adequate strain for the production of hyaluronidase. This strain was identified as Streptococcus milleri, based on its various biological properties. The enzyme produced in the culture supernatant of anaerobic culture was purified to homogeneity by sequential procedures including ammonium sulfate precipitation, ionexchange chromatography, and gel filtration. The specific activity increased 15,000 fold and the recovery of the enzyme activity was 21.3%. The molecular weight was 100,000 and its isoelectric point was 9.3. The optimum pH for the activity was 6.0. Heating of the enzyme at 60℃ for 5 minutes resulted in complete inactivation. The enzyme activity was inhibited strongly by Zn^<2+>, Hg^<2+>, and Cu^<2+>, while Ca^<2+>, Mg^<2+>, Fe^<2+>, Co^<2+>, Mn^<2+>, and EDTA had no effect. The enzyme was active against hyaluronic acid, however, chondroitin sulfate, chondroitin sulfate A, B, and C were not degraded by this enzyme. In the enzymatic products of hyaluronic acid, unsaturated disaccharides were detected by the methods of gel filtration and paper chromatography.},
 pages = {176--184},
 title = {Streptococcus milleriのヒアルロニダーゼの精製とその性状},
 volume = {14},
 year = {1988}
}