@article{oai:mdu.repo.nii.ac.jp:00001381,
 author = {NAKAMURA, TAKESHI and KIUCHI, NAOTO and FUJIMURA, SETSUO},
 issue = {2},
 journal = {松本歯学},
 month = {Dec},
 note = {application/pdf, Leucine aminopeptidase was purified from cell-free extracts of Actinomyces viscosus ATCC 19246 and some properties were investigated. The enzyme had a molecular weight of 65,000 and its isoelectric point was 4.0. Optimum pH was found at 7.0. The enzyme was quite labile over 40℃. It was sensitive to inhibition by diisopropylfluorophosphate, phenylmethane sulfonylfluoride, or tosyl-L-lysine chloromethyl ketone. Inhibition by urea was also obvious and this inhibition was found to be irreversible. Ca^<2+>, Mg^<2+>, Mn^<2+> or Co^<2+> had no no effect on the activity. Leucine-P-nitroanilide was the most suitable substrate among the tested synthetic substrates.},
 pages = {130--135},
 title = {Purification and Partial Characterization of Leucine Aminopeptidase from Actinomyces viscosus},
 volume = {10},
 year = {1984}
}