@article{oai:mdu.repo.nii.ac.jp:00001285,
 author = {柴田, 幸永 and 志村, 隆二 and 藤村, 節夫 and 中村, 武},
 issue = {3},
 journal = {松本歯学},
 month = {Dec},
 note = {application/pdf, When 8 strains of B. intermedius were isolated from pus samples collected from the human oral lesions and examined for their DNase production on DNA-TBO agar plates, it was found that all the strains had DNase activity. DNase was purified partially from the cell extract of one of those strains, LM-4, and its enzymatic properties were studied. Molecular weight was estimated to be 52,000 and isoelectric point was 7.2. Optium pH for the activity was around 7.0. The enzyme was activated by Mg^<2+> or Fe^<2+>, and inhibited by EDTA. The DNase hydrolized both denatured DNA and RNA, indicating that this DNase may be a non-specific nuclease.},
 pages = {293--301},
 title = {Bacteroides intermediusの核酸分解酵素(DNase)の精製とその性状},
 volume = {12},
 year = {1986}
}