Generation of plasma kinin by three types of protease isolated from Porphyromonas gingivalis 381

• Published in: Archives of oral biology Vol. 37; no. 10; p. 859
• Main Authors: Hinode, D, Nagata, A, Ichimiya, S, Hayashi, H, Morioka, M, Nakamura, R
• Format: Journal Article
• Language: English
• Published: England 01-10-1992
• Subjects: Bradykinin - metabolism; Endopeptidases - metabolism; Kallikreins - metabolism; Kinins - metabolism; Periodontal Diseases - enzymology; Periodontal Diseases - microbiology; Porphyromonas gingivalis - enzymology
• ISSN: 0003-9969
• DOI: 10.1016/0003-9969(92)90120-W

Three types of protease (A, B and C) isolated from the culture supernatant of Porphyromonas gingivalis 381 had peculiar activities on kinin generation from high molecular-weight kininogen in vitro. Protease C released bradykinin from the kininogen in a reaction mixture containing 2 mM dithiothreitol, but A and B did not. However, the activity of degrading bradykinin was much stronger in protease A and B than in C. These findings suggest that only protease C shows plasma kallikrein activity.