@phdthesis{oai:shinshu.repo.nii.ac.jp:00023621,
 author = {Matsuo, Kazuko and Kiso, Akiko and Shibata, Yukinaga and Hasegawa, Hiromasa and Fujimura, Setsuo and 松尾, 和子 and 木曽, 有紀子 and 柴田, 幸永 and 長谷川, 博雅 and 藤村, 節夫},
 month = {2015-07-06},
 note = {Formation, cellular locations, isolation and enzymatic propertiesof PTP of Porphyromonas gingivalis, an anaerobic periodontalpathogen were investigated.Almost all activities of this enzyme were detected in the crudeextract of the cell, but the other bacterial fractions such as culturefluids, envelopes and vesicles were not found to contain PTP.PTP was purified from the crude extract prepared by sonicationand centrifugation through five steps including concentration, ionexchange chromatography, gel filtration, hydrophobic interactionchromatography and isoelectric focusing to homogeneity.The enzyme was a serine enzyme since it was inhibited stronglyby Pefabloc SC, diisopropyl fluorophosphate and3,4-dichloroisocoumarin. It hydrolyzed H-Ala-Ala-Pro-pNA andH-Ala-Phe-Pro-pNA. The molecular mass was determined as 45kDa and isoelectric point was 5.7.Optimum pH was moderately broad, and maximum activity wasobserved in the range of pH 7.0 to 9.0.The residual activity after heating at 50℃ for 5 min was 29%,but heating at 60℃ resulted in complete loss of the activity., 2014, application/pdf, 甲第167号},
 school = {松本歯科大学},
 title = {Formation, isolation and characterization of a prolyl tripeptidyl peptidase of Porphyromonas gingivalis},
 year = {}
}