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+.

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