title: Purification and characterization of glycylprolyl aminopeptidase from Bacteroides gingivalis.
abstract: A glycylprocyl aminopeptidase from cell extracts of Bacteriodes gingivalis 381 was purified 1058-fold by hydrophobic adsorbent, HPLC anion exchange, and HPLC gel filtration column chromatography. The final enzyme preparation was homogeneous with a molecular weight of 75,000 daltons by SDS-PAGE, and the isoelectric point was 6.2. The optimum pH of the enzyme was 8.0, and the enzyme activity was inhibited by DFP Ni2+ and Hg2+.
authors.forename: T
authors.initials: T
authors.lastname: Miyauchi
authors.forename: M
authors.initials: M
authors.lastname: Hayakawa
authors.forename: Y
authors.initials: Y
authors.lastname: Abiko
mesh_terms: D000626:Aminopeptidases / Q000032:analysis / Q000302:isolation & purification*; D001439:Bacteroides / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D010510:Periodontal Diseases / Q000382:microbiology*
chemical_list: D000626:Aminopeptidases; C018085:glycylproline dipeptidyl aminopeptidase