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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Miyauchi et al. (1989) studied this question.
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