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. 1989 Aug;57(8):2522–2528. doi: 10.1128/iai.57.8.2522-2528.1989

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

P K Barua 1, M E Neiders 1, A Topolnycky 1, J J Zambon 1, H Birkedal-Hansen 1
PMCID: PMC313480  PMID: 2744859

Abstract

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%).

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Selected References

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