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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Purification of an 80,000-Mr glycylprolyl peptidase from Bacteroides gingivalis.

An enzyme from Bacteroides gingivalis SUNYAB A7A1-28 that hydrolyzes the synthetic peptide glycyl-L-proline 4-methoxy-beta-naphthylamide was purified 1,040-fold by urea extraction, gel filtration, ion-exchange chromatography, and fast protein liquid chromatography. The molecular weight of the enzyme was 80,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 75,000 as determined by gel filtration. The optimum pH for the hydrolysis of glycyl-L-proline 4-methoxy-beta-naphthylamide was 7.5 to 8. 5. The enzyme activity was inhibited by the serine protease inhibitors diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride by 82.5 and 78%, respectively. The activity was also inhibited by Hg2+ (55.6%) and Zn2+ (45%).[1]


  1. Purification of an 80,000-Mr glycylprolyl peptidase from Bacteroides gingivalis. Barua, P.K., Neiders, M.E., Topolnycky, A., Zambon, J.J., Birkedal-Hansen, H. Infect. Immun. (1989) [Pubmed]
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