[A study of gingivain from extracellular vesicles of Porphyromonas gingivalis W50: purification and cytotoxic characterization].
Gingivain was purified from extracellular vesicles of Porphyromonas gingivalis W50 with high performance liquid chromatography (HPLC) and its cytotoxic characterization on L929 cell line was examined. The result showed that gingivain might belong to systeine proteinases. The molecular weight of gingivain was about 27,800 unit by HPLC in which there might be one or two peptides being 10,900 unit, the enzyme was activated by Ca2+ and thiol-containing agents such as dithiothycitol and inhibited by Na-4-tosyl-L-lysine chioromethyl and EDTA. The maximum activity of the enzyme were found at pH 7.5, purified gingivain was toxic to L929 cell line at the content of 10 micrograms/ml. The study indicates that gingivain carried by vesicles might be more important in bacterial toxic activities.
Ni
L
L
Stomatological College, Fourth Military Medical University, Xi'an.
Shi
J
J
Liu
Z
Z
D001426:Bacterial Proteins; D002460:Cell Line; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000633:toxicity*; D006801:Humans; D008970:Molecular Weight; D016966:Porphyromonas gingivalis / Q000737:chemistry*
D001426:Bacterial Proteins; D003546:Cysteine Endopeptidases; C067046:gingivain; C091975:prtR protein, Porphyromonas gingivalis W50