Generation of plasma kinin by three types of protease isolated from Porphyromonas gingivalis 381.
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.
Hinode
D
D
Department of Preventive Dentistry, School of Dentistry, University of Tokushima, Japan.
Nagata
A
A
Ichimiya
S
S
Hayashi
H
H
Morioka
M
M
Nakamura
R
R
D001920:Bradykinin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D007610:Kallikreins / Q000378:metabolism; D007705:Kinins / Q000378:metabolism*; D010510:Periodontal Diseases / Q000201:enzymology / Q000382:microbiology; D016966:Porphyromonas gingivalis / Q000201:enzymology*
D007705:Kinins; D010450:Endopeptidases; D007610:Kallikreins; D001920:Bradykinin